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1-(1,3-benzodioxol-5-yloxy)propan-2-one + pyruvate
? + CO2
1-(2-bromo-5-hydroxyphenoxy)propan-2-one + pyruvate
? + CO2
-
-
-
?
1-(naphthalen-2-yloxy)propan-2-one + pyruvate
? + CO2
-
-
-
?
1-(phenylsulfanyl)propan-2-one + pyruvate
? + CO2
-
-
-
?
1-naphthaldehyde + pyruvate
(1R)-1-hydroxy-1-(naphthalen-1-yl)propan-2-one + CO2
1-phenoxypropan-2-one + pyruvate
3-hydroxy-3-methyl-4-phenoxybutan-2-one + CO2
1-phenoxypropan-2-one + pyruvate
? + CO2
-
-
-
?
2 butane-2,3-dione
acetylacetoin + acetoin
2 pyruvate
(S)-acetoin + 2 CO2
2 pyruvate
(S)-acetolactate + CO2
2 pyruvate
2-acetolactate + CO2
2-acetyl-2-hydroxycyclohexanone + pyruvate
1-(1-hydroxycyclohexyl)ethanone + CO2
-
-
-
-
?
2-bromobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-bromophenyl)propan-2-one + CO2
2-chlorobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-chlorophenyl)propan-2-one + CO2
2-chlorobenzaldehyde + pyruvate
? + CO2
-
-
-
?
2-fluorobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-fluorophenyl)propan-2-one + CO2
-
-
-
-
?
2-hydroxybenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-hydroxyphenyl)propan-2-one + CO2
-
-
-
-
?
2-iodobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-iodophenyl)propan-2-one + CO2
-
-
-
-
?
2-methoxybenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-methoxyphenyl)propan-2-one + CO2
-
-
-
-
?
2-methylbenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-methylphenyl)propan-2-one + CO2
-
-
-
-
?
2-naphthaldehyde + pyruvate
(1R)-1-hydroxy-1-(naphthalen-2-yl)propan-2-one + CO2
-
-
-
-
?
2-nitrobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-nitrophenyl)propan-2-one + CO2
-
-
-
-
?
2-oxobutanoate + lactylthiamine diphosphate
acetohydroxybutanoate + ?
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
2-oxobutanoate + pyruvate
2-propionyl-2-hydroxybutanoate + ?
-
reaction catalyzed by mutant V375A
-
-
?
2-oxobutyrate
2-ethyl-2-hydroxy-3-oxopentanoate + CO2
-
-
-
ir
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
2-oxobutyrate + pyruvate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
2-oxoisovalerate
isobutyraldehyde + CO2
2-oxopropyl 4-bromobenzoate + pyruvate
? + CO2
-
-
-
?
3,4-dihydronaphthalen-2(1H)-one + pyruvate
? + CO2
-
-
-
?
4-(tert-butyl)benzaldehyde + pyruvate
(R)-1-hydroxy-1-(4-(tert-butyl)phenyl)propan-2-one + CO2
-
-
-
-
?
4-ethoxybenzaldehyde + pyruvate
(R)-1-hydroxy-1-(4-ethoxyphenyl)propan-2-one + CO2
-
-
-
-
?
4-ethylbenzaldehyde + pyruvate
(R)-1-hydroxy-1-(4-ethylphenyl)propan-2-one + CO2
-
-
-
-
?
4-hydroxybenzaldehyde + pyruvate
? + CO2
-
-
-
?
4-isopropylbenzaldehyde + pyruvate
(R)-1-hydroxy-1-(4-isopropylphenyl)propan-2-one + CO2
-
-
-
-
?
4-phenylbenzaldehyde + pyruvate
(R)-1-hydroxy-1-(4-ethylphenyl)propan-2-one + CO2
-
-
-
-
?
butane-2,3-dione + benzaldehyde
? + CO2
-
-
-
-
?
butane-2,3-dione + pyruvate
acetylacetoin + CO2
-
-
-
-
?
cyclohexane-1,2-dione + pyruvate
? + CO2
-
-
-
?
cyclohexanone + pyruvate
? + CO2
-
-
-
?
dihydro-2H-pyran-3(4H)-one + pyruvate
1-(3-hydroxytetrahydro-2H-pyran-3-yl)ethanone + CO2
-
-
-
-
?
dihydro-2H-pyran-3(4H)-one + pyruvate
? + CO2
-
-
-
?
ethyl 3-oxobutanoate + pyruvate
? + CO2
-
-
-
?
hexan-3,4-dione + pyruvate
? + CO2
-
-
-
?
hexane-3,4-dione + pyruvate
(S)-3-ethyl-3-hydroxyhexane-2,4-dione + CO2
-
-
-
-
?
hydroxypyruvate
? + CO2
-
-
-
-
?
methylpyruvate + benzaldehyde
(S)-acetoin + CO2
-
-
-
-
?
methylpyruvate + pyruvate
? + CO2
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
pyruvate
2-acetolactate + CO2
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
pyruvate + 2-oxobutyrate
(S)-acetohydroxybutyrate + CO2
-
stereospecific reaction
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
pyruvate + 2-oxobutyrate
2-acetohydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
pyruvate + cyclohexane-1,2-dione
?
-
although cyclohexane-1,2-dione is a substrate of a C-C bond-cleavage reaction catalyzed by CDH, EC 3.7.1.11, wild-type CDH is unable to catalyze C-C bond formation (carboligation) using pyruvate as acyl anion donor and cyclohexane-1,2-dione as the acceptor. The formation of a tertiary alcohol is catalyzed by the enzyme double mutant CDH-H28A/N484A
-
-
?
pyruvate + O2
peracetate + CO2
-
isozymes AHAS II and AHAS III, oxygen-consuming side reaction
-
-
?
pyruvate + pyruvate
2-acetolactate + CO2
additional information
?
-
1-(1,3-benzodioxol-5-yloxy)propan-2-one + pyruvate
? + CO2
-
-
-
?
1-(1,3-benzodioxol-5-yloxy)propan-2-one + pyruvate
? + CO2
-
-
-
?
1-naphthaldehyde + pyruvate
(1R)-1-hydroxy-1-(naphthalen-1-yl)propan-2-one + CO2
-
-
-
-
?
1-naphthaldehyde + pyruvate
(1R)-1-hydroxy-1-(naphthalen-1-yl)propan-2-one + CO2
-
-
-
-
?
1-phenoxypropan-2-one + pyruvate
3-hydroxy-3-methyl-4-phenoxybutan-2-one + CO2
-
-
-
-
?
1-phenoxypropan-2-one + pyruvate
3-hydroxy-3-methyl-4-phenoxybutan-2-one + CO2
-
-
-
-
?
2 butane-2,3-dione
acetylacetoin + acetoin
-
homocoupling of butane-2,3-dione by the wild-type enzyme, no activity with mutant H28A/N484A
-
-
?
2 butane-2,3-dione
acetylacetoin + acetoin
-
homocoupling of butane-2,3-dione by the wild-type enzyme, no activity with mutant H28A/N484A
-
-
?
2 pyruvate
(S)-acetoin + 2 CO2
-
enzymatic formation of highly enantioenriched acetoin from two molecules of pyruvate occurs without the release of acetaldehyde or acetolactate
87-90%ee
-
?
2 pyruvate
(S)-acetoin + 2 CO2
-
in the absence of aldehydes, CDH catalyzes the decarboxylation and homocoupling of pyruvate to provide (S)-acetoin (3-hydroxybutan-2-one) with remarkably high enantioselectivity (up to 93%ee)
-
-
?
2 pyruvate
(S)-acetoin + 2 CO2
-
in the absence of aldehydes, CDH catalyzes the decarboxylation and homocoupling of pyruvate to provide (S)-acetoin (3-hydroxybutan-2-one) with remarkably high enantioselectivity (up to 93%ee)
-
-
?
2 pyruvate
(S)-acetoin + 2 CO2
-
enzymatic formation of highly enantioenriched acetoin from two molecules of pyruvate occurs without the release of acetaldehyde or acetolactate
87-90%ee
-
?
2 pyruvate
(S)-acetolactate + CO2
-
-
-
?
2 pyruvate
(S)-acetolactate + CO2
-
-
-
?
2 pyruvate
(S)-acetolactate + CO2
-
-
-
?
2 pyruvate
(S)-acetolactate + CO2
-
-
-
?
2 pyruvate
(S)-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
acetohydroxyacid synthase is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
60fold higher specificity for 2-ketobutyrate over pyruvate as acceptor
-
-
?
2 pyruvate
2-acetolactate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
AHAS catalyzes the first common step in the biosynthetic pathway of the branched-amino acids leucine, isoleucine, and valine
-
-
?
2 pyruvate
2-acetolactate + CO2
condensation reaction
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?, ir
2 pyruvate
2-acetolactate + CO2
catalytic subunit ilvG shows positive cooperativity towards substrate and cofactors
-
-
?
2 pyruvate
2-acetolactate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
catalytic subunit ilvG shows positive cooperativity towards substrate and cofactors
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?, ir
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
product decarboxylates spontaneously to final product acetoin (i.e. 3-hydroxybutanone), which is a major product at temperatures below 80°C. Acetolactate synthase ALS, which is involved in branched-chain amino acid biosynthesis, is responsible and deletion of the Als gene abolishes acetoin production
-
?
2 pyruvate
2-acetolactate + CO2
the enzyme produces 2-acetolactate in a temperature-dependent manner
-
-
?
2 pyruvate
2-acetolactate + CO2
activated enzyme ALS catalyzes the condensation and decarboxylation of two pyruvates to one 2-acetolactate
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2-bromobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-bromophenyl)propan-2-one + CO2
-
-
-
-
?
2-bromobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-bromophenyl)propan-2-one + CO2
-
-
-
-
?
2-chlorobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-chlorophenyl)propan-2-one + CO2
-
-
-
-
?
2-chlorobenzaldehyde + pyruvate
(R)-1-hydroxy-1-(2-chlorophenyl)propan-2-one + CO2
-
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
-
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
-
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
-
60fold higher specificity for 2-ketobutyrate over pyruvate as acceptor
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
-
-
-
?
2-oxobutanoate + pyruvate
2-hydroxy-2-methyl-3-oxopentanoate + CO2
-
-
-
-
?
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
-
-
-
-
?
2-oxoisovalerate
isobutyraldehyde + CO2
-
-
-
?
2-oxoisovalerate
isobutyraldehyde + CO2
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
-
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
-
stereospecific reaction
-
-
?
pyruvate
(S)-2-acetolactate + CO2
-
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate
(S)-2-acetolactate + CO2
stereospecific reaction
-
-
?
pyruvate
(S)-2-acetolactate + CO2
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, overview
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
r
pyruvate
2-acetolactate + CO2
-
first step in the biosynthesis of valine, overview
-
-
r
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, regulation, overview
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
r
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
r
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
the expression is negatively controlled by Val. Leu and Ile slightly stimulate the enzyme production
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu, Ile and Val
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu
-
-
?
pyruvate
?
-
production of isoenzyme AHS I is under multivalent control by Val and Leu, production of isoenzyme AHS II is under multivalent control by Ile, Val and Leu
-
-
?
pyruvate
?
-
isoenzyme AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme I is regulated by Leu and Val
-
-
?
pyruvate
?
-
key enzyme in synthesis of branched-chain amino acids
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
constitutive high expression, the enzyme is active only under conditions of pyruvate excess
-
-
?
pyruvate
?
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu, Ile and Val
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu
-
-
?
pyruvate
?
-
isoenzyme AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme I is regulated by Leu and Val
-
-
?
pyruvate
?
-
the enzyme plays a role in not only preventing intracellular acidification but also supplying alpha-acetolactate as an intermediate of branched chain amino acids biosynthesis
-
-
?
pyruvate
?
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
-
-
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
-
isoenzyme I shows no product preference, isoenzymes II and III form acetohydroxybutanoate at 180fold and 60fold faster rates, respectively than acetolactate
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
-
much higher affinity for 2-oxobutanoate than for pyruvate
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
-
preference for 2-ketobutanoate at the second substrate site
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
-
isoenzyme I shows no product preference, isoenzymes II and III form acetohydroxybutanoate at 180fold and 60fold faster rates, respectively than acetolactate
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
-
no activity
-
-
?
pyruvate + 2-oxobutanoate
acetohydroxybutanoate
-
preference for 2-ketobutanoate at the second substrate site
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
asymmetric benzoin condensation between benzaldehyde and pyruvate
(R)-configuration with over 99% ee
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee)
i.e. (R)-1-hydroxy-1-phenylpropan-2-one
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
asymmetric benzoin condensation between benzaldehyde and pyruvate
(R)-configuration with over 99% ee
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee)
i.e. (R)-1-hydroxy-1-phenylpropan-2-one
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, benzaldehyde is an artificial substrate, especially of mutants of isozyme AHAS II residues Phe109, Met250, Arg276 and Trp464
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, isozymes AHAS I and II
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
pyruvate + pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate + pyruvate
2-acetolactate + CO2
-
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, EC 3.7.1.11, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
additional information
?
-
-
in addition to its physiological C-C bond-cleavage activity, CDH catalyzes the asymmetric cross-benzoin reaction of a broad variety of aromatic aldehydes and pyruvate. In the case of the sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde, the respective 2-hydroxyketone products are obtained in high yield. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields, enzyme substrate specificity and enantioselectivity, overview
-
-
?
additional information
?
-
-
ThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) is able to form (S)-acetoin with particularly high enantioselectivity (up to 95%ee) by all three possible pathways: homocoupling of pyruvate, homocoupling of acetaldehyde, or cross-coupling of acetaldehyde (as acceptor) and pyruvate (as donor), high enantioselectivity in the CDH-catalyzed formation of (S)-acetoin. An unprecedented non-acetolactate pathway for the homocoupling of pyruvate explains the high enantioselectivity in the CDH-catalyzed formation of (S)-acetoin, enzymatic formation of highly enantioenriched acetoin from two molecules of pyruvate occurs without the release of acetaldehyde or acetolactate, competition assay, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, EC 3.7.1.11, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
additional information
?
-
-
in addition to its physiological C-C bond-cleavage activity, CDH catalyzes the asymmetric cross-benzoin reaction of a broad variety of aromatic aldehydes and pyruvate. In the case of the sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde, the respective 2-hydroxyketone products are obtained in high yield. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields, enzyme substrate specificity and enantioselectivity, overview
-
-
?
additional information
?
-
-
ThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) is able to form (S)-acetoin with particularly high enantioselectivity (up to 95%ee) by all three possible pathways: homocoupling of pyruvate, homocoupling of acetaldehyde, or cross-coupling of acetaldehyde (as acceptor) and pyruvate (as donor), high enantioselectivity in the CDH-catalyzed formation of (S)-acetoin. An unprecedented non-acetolactate pathway for the homocoupling of pyruvate explains the high enantioselectivity in the CDH-catalyzed formation of (S)-acetoin, enzymatic formation of highly enantioenriched acetoin from two molecules of pyruvate occurs without the release of acetaldehyde or acetolactate, competition assay, mechanism, overview
-
-
?
additional information
?
-
-
enzyme additionallly displays 2-ketoisovalerate decarboxylase activity
-
-
?
additional information
?
-
enzyme additionallly displays 2-ketoisovalerate decarboxylase activity
-
-
?
additional information
?
-
enzyme AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. The enzyme also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
-
-
?
additional information
?
-
-
enzyme AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. The enzyme also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
-
-
?
additional information
?
-
-
acetolactate synthase AlsS is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro
-
-
?
additional information
?
-
acetolactate synthase AlsS is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro
-
-
?
additional information
?
-
acetolactate synthase AlsS is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro
-
-
?
additional information
?
-
enzyme AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. The enzyme also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
mechanism of expression regulation, overview
-
-
?
additional information
?
-
-
acetohydroxybutyrate is preferably formed, isozyme AHAS I can also form peracetate from synthetic acetolactate
-
-
?
additional information
?
-
-
substrate specificity ratios of isozymes I-III, substrate recognition mechanism, overview
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
the specificity of AHAS for 2-ketoacids as acceptor substrates is due to an arginine residue which probably interacts with the carboxylate of the second substrate, e.g., Arg276 in AHAS II. Mutants altered at this arginine can utilize aromatic aldehydes as second substrate and form chiral arylacyl carbinols. Mechanistically, carboligation occurs after rate-determining formation of hydroxyethyl-thiamine diphosphate. A faster rate constant for product release when the alkyl group derived from the acceptor substrate is ethyl compared to methyl plays a major role in product specificity. The crucial role of a Trp residue, i.e. Trp 464 in AHAS II, in determining specificity may be due to control of a conformational change involved in product release rather than to affinity for 2-ketobutyrate
-
-
?
additional information
?
-
-
a valine and a phenylalanine residue hydrophobically interact with the methyl substituent of pyruvate. A mutation of either Val375 or Phe109 is detrimental for unimolecular catalytic steps in which tetrahedral intermediates are involved, such as substrate addition to the cofactor and product liberation. Val375 and Phe109 to not only conjointly mediate substrate binding and specificity but moreover to ensure a proper orientation of the donor substrate and intermediates for correct orbital alignment in multiple transition states
-
-
?
additional information
?
-
-
isozyme I is not specific for 2-oxobutanoate over pyruvate as an acceptor substrate. Residues Gln480 and Met476 in AHAS I replace the Trp and Leu residues conserved in other acetohydroxyacid synthases and lead to accelerated ligation and product release steps. This difference in kinetics accounts for the unique specificity, reversibility and allosteric response of AHAS I
-
-
?
additional information
?
-
-
residue Glu47 has a crucial catalytic role for it in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation. Either the transient oxyanion on the acceptor carbonyl is stabilized by H-bonding to the glutamine side chain, or carboligation involves glutamine tautomerization and the elementary reactions of addition and protonation occur in a concerted manner. Gln110 and Glu47 have global catalytic roles, being engaged in all major bond-breaking and bond-making steps. Lys159 has a minor effect on the kinetics and specificity of isoform AHAS II, far less than does Arg276,which influences the specificity for a 2-ketoacid as a second substrate. His251 has a large effect on donor substrate binding, but this effect masks any other effects of replacement of His251
-
-
?
additional information
?
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of pyruvate and 2-oxobutyrate, respectively. Substrate specificities of isozymes: isozymes AHAS II and AHAS III prefer 2-oxobutyrate as the second substrate whereas such selectivity is not observed in case of isozyme AHAS I. Isozymes AHAS I and AHAS II are capable of self condensing 2-oxobutyrate to form 2-ethyl-2-hydroxy-3-oxopentanoate
-
-
?
additional information
?
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of pyruvate and 2-oxobutyrate, respectively. Substrate specificities of isozymes: isozymes AHAS II and AHAS III prefer 2-oxobutyrate as the second substrate whereas such selectivity is not observed in case of isozyme AHAS I. Isozymes AHAS I and AHAS II are capable of self condensing 2-oxobutyrate to form 2-ethyl-2-hydroxy-3-oxopentanoate
-
-
?
additional information
?
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of pyruvate and 2-oxobutyrate, respectively. Substrate specificities of isozymes: isozymes AHAS II and AHAS III prefer 2-oxobutyrate as the second substrate whereas such selectivity is not observed in case of isozyme AHAS I. Isozymes AHAS I and AHAS II are capable of self condensing 2-oxobutyrate to form 2-ethyl-2-hydroxy-3-oxopentanoate
-
-
?
additional information
?
-
-
regulatory role of the proteins of the phosphoenolpyruvate:carbohydrate phosphotransferase system, requirement of the dephospho-form of enzyme IIANtr, encoded by gene ptsN, for derepression of Escherichia coli K-12 ilvBN expression, overview
-
-
?
additional information
?
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
detection of nonenzymatic acetoin formation from acetolactate in the assay
-
-
?
additional information
?
-
-
detection of nonenzymatic acetoin formation from acetolactate in the assay
-
-
?
additional information
?
-
-
detection of nonenzymatic acetoin formation from acetolactate in the assay
-
-
?
additional information
?
-
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively
-
-
?
additional information
?
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively
-
-
?
additional information
?
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively
-
-
?
additional information
?
-
-
the enzyme can act in anabolic or in catabolic function, the first enzyme contains the conserved motif 372RFDDR376, while the latter does not, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
-
-
?
additional information
?
-
-
acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
-
-
?
additional information
?
-
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively
-
-
?
additional information
?
-
non-enzymatic decarboxylation of acetolactate to acetoin
-
-
?
additional information
?
-
-
non-enzymatic decarboxylation of acetolactate to acetoin
-
-
?
additional information
?
-
assay method with indirect quantitation of alpha-acetolactate by measuring acetoin formation
-
-
?
additional information
?
-
-
assay method with indirect quantitation of alpha-acetolactate by measuring acetoin formation
-
-
?
additional information
?
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
the product of this enzyme-catalyzed reaction is either 2-acetolactate or 2-aceto-2-hydroxybutyrate obtained from self-condensation of pyruvate or condensation of puruvate and 2-ketobutyrate, respectively
-
-
?
additional information
?
-
-
sll1981 functions as L-myo-inositol 1-phosphate synthase, MIPS, EC 5.5.1.4, overview
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
non-enzymatic decarboxylation of acetolactate to acetoin
-
-
?
additional information
?
-
-
non-enzymatic decarboxylation of acetolactate to acetoin
-
-
?
additional information
?
-
non-enzymatic decarboxylation of acetolactate to acetoin
-
-
?
additional information
?
-
YerE might posses the ability to activate non-sugar ketones for cross-benzoin condensations, performing enzymatic aldehyde-ketone cross-benzoin condensations
-
-
?
additional information
?
-
asymmetric intermolecular crossed aldehyde-ketone condensation through enzymatic carboligation reaction. Carboligation reactions catalyzed by the ThDP-dependent enzyme YerE with pyruvate and an acceptor substrate can lead to tertiary alcohols, (R)-phenylacetylcarbinol derivatives, (S )-acetolactate, and (S)-acetoin, overview
-
-
?
additional information
?
-
YerE might posses the ability to activate non-sugar ketones for cross-benzoin condensations, performing enzymatic aldehyde-ketone cross-benzoin condensations
-
-
?
additional information
?
-
asymmetric intermolecular crossed aldehyde-ketone condensation through enzymatic carboligation reaction. Carboligation reactions catalyzed by the ThDP-dependent enzyme YerE with pyruvate and an acceptor substrate can lead to tertiary alcohols, (R)-phenylacetylcarbinol derivatives, (S )-acetolactate, and (S)-acetoin, overview
-
-
?
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2 pyruvate
2-acetolactate + CO2
2-oxobutyrate
2-ethyl-2-hydroxy-3-oxopentanoate + CO2
-
-
-
ir
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
2-oxobutyrate + pyruvate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
2-oxoisovalerate
isobutyraldehyde + CO2
pyruvate
(S)-2-acetolactate + CO2
pyruvate
2-acetolactate + CO2
pyruvate + 2-oxobutyrate
(S)-acetohydroxybutyrate + CO2
-
stereospecific reaction
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
pyruvate + 2-oxobutyrate
2-acetohydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
pyruvate + pyruvate
2-acetolactate + CO2
additional information
?
-
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
acetohydroxyacid synthase is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
AHAS catalyzes the first common step in the biosynthetic pathway of the branched-amino acids leucine, isoleucine, and valine
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?, ir
2 pyruvate
2-acetolactate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?, ir
2 pyruvate
2-acetolactate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
the enzyme produces 2-acetolactate in a temperature-dependent manner
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
2 pyruvate
2-acetolactate + CO2
-
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2 pyruvate
2-acetolactate + CO2
-
-
-
?
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
-
-
-
-
?
2-oxoisovalerate
isobutyraldehyde + CO2
-
-
-
?
2-oxoisovalerate
isobutyraldehyde + CO2
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
-
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate
(S)-2-acetolactate + CO2
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, overview
-
-
?
pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate
2-acetolactate + CO2
-
first step in the biosynthesis of valine, overview
-
-
r
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, regulation, overview
-
-
?
pyruvate
2-acetolactate + CO2
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
first committed step in the biosynthesis of valine and leucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
r
pyruvate
2-acetolactate + CO2
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
the expression is negatively controlled by Val. Leu and Ile slightly stimulate the enzyme production
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu, Ile and Val
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu
-
-
?
pyruvate
?
-
production of isoenzyme AHS I is under multivalent control by Val and Leu, production of isoenzyme AHS II is under multivalent control by Ile, Val and Leu
-
-
?
pyruvate
?
-
isoenzyme AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme I is regulated by Leu and Val
-
-
?
pyruvate
?
-
key enzyme in synthesis of branched-chain amino acids
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
constitutive high expression, the enzyme is active only under conditions of pyruvate excess
-
-
?
pyruvate
?
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu, Ile and Val
-
-
?
pyruvate
?
-
isoenzyme II is regulated by Leu
-
-
?
pyruvate
?
-
isoenzyme AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
isoenzyme I is regulated by Leu and Val
-
-
?
pyruvate
?
-
the enzyme plays a role in not only preventing intracellular acidification but also supplying alpha-acetolactate as an intermediate of branched chain amino acids biosynthesis
-
-
?
pyruvate
?
-
catabolic enzyme is involved in 2,3-butanediol pathway
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate
?
-
first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
first committed step in the biosynthesis of isoleucine
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
-
-
-
-
?
pyruvate + 2-oxobutyrate
acetohydroxybutyrate + CO2
-
-
-
-
?
pyruvate + pyruvate
2-acetolactate + CO2
-
-
-
-
?
pyruvate + pyruvate
2-acetolactate + CO2
-
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, EC 3.7.1.11, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
additional information
?
-
-
the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, EC 3.7.1.11, and the asymmetric benzoin condensation between benzaldehyde and pyruvate
-
-
?
additional information
?
-
enzyme AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. The enzyme also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
-
-
?
additional information
?
-
-
enzyme AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. The enzyme also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
-
-
?
additional information
?
-
enzyme AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. The enzyme also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
mechanism of expression regulation, overview
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
regulatory role of the proteins of the phosphoenolpyruvate:carbohydrate phosphotransferase system, requirement of the dephospho-form of enzyme IIANtr, encoded by gene ptsN, for derepression of Escherichia coli K-12 ilvBN expression, overview
-
-
?
additional information
?
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
the enzyme can act in anabolic or in catabolic function, the first enzyme contains the conserved motif 372RFDDR376, while the latter does not, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
additional information
?
-
acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
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additional information
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acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids
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additional information
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non-enzymatic decarboxylation of acetolactate to acetoin
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additional information
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non-enzymatic decarboxylation of acetolactate to acetoin
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additional information
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AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
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additional information
?
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AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
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-
?
additional information
?
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AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
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?
additional information
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YerE might posses the ability to activate non-sugar ketones for cross-benzoin condensations, performing enzymatic aldehyde-ketone cross-benzoin condensations
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additional information
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YerE might posses the ability to activate non-sugar ketones for cross-benzoin condensations, performing enzymatic aldehyde-ketone cross-benzoin condensations
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(2E)-3,3'-dioxo-1,1',3,3'-tetrahydro-2,2'-biindole-5,5'-disulfonate
-
inhibition profile and inhibition of root growth, overview
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl benzoate
-
-
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl phenylacetate
-
-
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl prop-2-enoate
-
-
1-(4,6-dimethoxypyrimidin-2-yl)-5-methoxymethyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
1-(4,6-dimethoxypyrimidin-2-yl)-5-methyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
1-(4,6-dimethoxypyrimidin-2-yl)-5-methylthio-N-(2-chloro-6-fluorophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
1-(4-chloro-6-methoxypyrimidin-2-yl)-5-methoxy-N-(2-methyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
-
-
1-methoxy-1-oxopropan-2-yl 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methyl[1,1'-biphenyl]-2-carboxylate
-
2'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
-
2,3-dichloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-(1,1-dihydroxyethyl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-(2,3-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2,3-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2,4-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2,4-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2,5-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2,5-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2-bromobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(2-bromophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2-chloro-4-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(2-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(2-chloroethoxy)-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-(2-chloroethoxy)-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-(2-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(3-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(3-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(3-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-(trifluoromethyl)benzoate
-
30% inhibition at 0.1 mM
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-chlorobenzoate
-
42.5% inhibition at 0.1 mM
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-fluorobenzoate
-
72% inhibition at 0.1 mM
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-methoxybenzoate
-
28% inhibition at 0.1 mM
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl benzoate
-
26% inhibition at 0.1 mM
2-(3-methoxyphenyl)-4-oxoquinazolin-3(4H)-yl 3-(trifluoromethyl)benzoate
-
73.2% inhibition at 0.1 mM
2-(3-methoxyphenyl)-4-oxoquinazolin-3(4H)-yl 3-chlorobenzoate
-
23.5% inhibition at 0.1 mM
2-(3-methoxyphenyl)-4-oxoquinazolin-3(4H)-yl 3-nitrobenzoate
-
94% inhibition at 0.1 mM
2-(4-bromo-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(4-chloro-2-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(4-chloro-2-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(4-chloro-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(4-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(4-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-(5-chloropyridin-3-yl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylbenzoic acid
-
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
2-(6-chloropyridin-3-yl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylbenzoic acid
-
2-(difluoromethoxy)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
2-amino-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
2-bromo-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-bromo-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-bromo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-butoxy-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-butyl-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-chloro-3-oxocyclohex-1-en-1-yl 3-(trifluoromethyl)benzoate
-
2-chloro-3-oxocyclohex-1-en-1-yl-3-(trifluoromethyl)benzoate
-
2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
-
2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoic acid
no inhibition by bensulfuron methyl. Feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern
2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoic acid ester
-
2-chloro-6-(methoxycarbonyl)-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
-
2-chloro-6-methoxycarbonyl-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
-
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
2-chloro-N-(4-chloro-3-[[(4-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]phenyl)acetamide
-
2-chloro-N-(4-chloro-3-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]phenyl)acetamide
-
2-chloro-N-([4-(methylamino)-6-[(1-methylethyl)sulfanyl]-1,3,5-triazin-2-yl]carbamoyl)benzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-chloro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-chloro-N-[[4-(ethylsulfanyl)-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-(ethylsulfanyl)-6-methoxy-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-(ethylsulfanyl)-6-methylpyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-(methylamino)-6-(methylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-chloro-N-[[4-methyl-6-(propylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
-
-
2-ethoxy-2-oxoethyl 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methyl[1,1'-biphenyl]-2-carboxylate
-
2-fluoro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-fluoro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-fluoro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-iodo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-iodo-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
2-methoxy-2-oxoethyl 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methyl[1,1'-biphenyl]-2-carboxylate
-
2-nitro-5-(phenylsulfonyl)phenyl 4-chlorobenzoate
-
2-oxoisovalerate
competitive
2-phenyl-3-[[3-(trifluoromethyl)benzoyl]oxy]quinazolin-4(3H)-one
-
2-phenyl-3-{[3-(trifluoromethyl)benzoyl]oxy}quinazolin-4-one
-
2-substituted-8-(4,6-dimethoxypyrimidin-2-yloxy)-4-methylphthalazin-1-one derivatives
-
synthesis of diverse derivatives and inhibitory potency, overview
-
2-[(2-chloroethoxy)methyl]-N-[(4-chloropyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-[(2-chloroethoxy)methyl]-N-[(4-methylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-3-methylphenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-4-methylphenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-5-methylphenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluorophenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-fluorophenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-methylphenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-fluorophenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-methylphenoxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(naphthalen-2-yloxy)benzoic acid
-
-
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-phenoxybenzoic acid
-
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(5-methylpyridin-3-yl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(naphthalen-2-yl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(pyridin-3-yl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(pyrimidin-5-yl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-(methylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethynylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-hydroxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-iodobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-nitrobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1-methylethoxy)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1H-pyrrol-1-yl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(2-methoxypyrimidin-5-yl)-4-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(3,5-dimethyl-1,2-oxazol-4-yl)-4-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(6-fluoropyridin-3-yl)-4-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(ethylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(furan-2-yl)-4-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(furan-3-yl)-4-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfonyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(phenylcarbonyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(propylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(trifluoromethoxy)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-iodobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-nitrobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-phenoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(1-methylethoxy)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(ethylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(methylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(phenylcarbonyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(propylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(trifluoromethyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-ethoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-iodobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-nitrobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-phenoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-propoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
2-[([1,1'-biphenyl]-4-yl)oxy]-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
-
2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]-N,N-dimethylbenzamide
-
-
3'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
-
3-(7H-cyclopenta[b]pyridin-5-yl)-N-[(2-nitrophenyl)sulfanyl]alanine
-
inhibition profile and inhibition of root growth, overview
3-Bromopyruvate
-
competitive to 2-oxobutanoate
3-phosphoglycerate
-
noncompetitive
3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4(3H)-one
-
3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4-one
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-2'-fluoro-5-methylbiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3',5'-difluoro-5-methylbiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3'-fluoro-5-methylbiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4',5-dimethylbiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4'-fluoro-5-methylbiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4'-methoxy-5-methylbiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methyl-4'-nitrobiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
3-[(4-nitrobenzoyl)oxy]quinazolin-4(3H)-one
-
3-[(4-nitrobenzoyl)oxy]quinazolin-4-one
-
4'-bromo-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
-
4'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybiphenyl-2-carboxylic acid
-
4'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
-
4-(cyclopropylcarbonyl)-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-1-methyl-1H-pyrazole-5-sulfonamide
-
i.e. K13030
4-acetyl-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-1-methyl-1H-pyrazole-5-sulfonamide
-
i.e. K13010
4-oxo-2-m-tolylquinazolin-3(4H)-yl 3-fluorobenzoate
-
9.5% inhibition at 0.1 mM
4-oxo-2-m-tolylquinazolin-3(4H)-yl 3-methylbenzoate
-
10.5% inhibition at 0.1 mM
4-oxo-2-m-tolylquinazolin-3(4H)-yl 4-chlorobenzoate
-
no inhibition at 0.1 mM
4-oxo-2-m-tolylquinazolin-3(4H)-yl 4-methylbenzoate
-
33% inhibition at 0.1 mM
4-oxo-2-m-tolylquinazolin-3(4H)-yl benzoate
-
40.5% inhibition at 0.1 mM
4-oxo-2-m-tolylquinazolin-3(4H)-yl-3-(trifluoromethyl)benzoate
-
9.5% inhibition at 0.1 mM
4-oxo-2-o-tolylquinazolin-3(4H)-yl 3-fluorobenzoate
-
30% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 2-methylbenzoate
-
16.5% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 3-chlorobenzoate
-
80.5% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 3-fluorobenzoate
-
26% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 3-methoxybenzoate
-
27% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 3-methylbenzoate
-
4% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 3-nitrobenzoate
-
91.5% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 4-chlorobenzoate
-
7.5% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl 4-methylbenzoate
-
18% inhibition at 0.1 mM
4-oxo-2-phenylquinazolin-3(4H)-yl benzoate
-
20.5% inhibition at 0.1 mM
5-amino-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-benzyl-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-bromo-2-([[(2-chlorophenyl)sulfonyl]carbamoyl]amino)pyrimidin-4-yl benzoate
-
-
5-bromo-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-chloro-1-(4-chlorophenyl)-3-methyl-N-((4-(trifluoromethoxy)phenyl)sulfonyl)-1H-pyrazole-4-carboxamide
-
5-chloro-1-(4-chlorophenyl)-3-methyl-N-(phenylsulfonyl)-1H-pyrazole-4-carboxamide
-
5-chloro-1-(4-chlorophenyl)-3-methyl-N-tosyl-1H-pyrazole-4-carboxamide
-
5-chloro-1-(4-chlorophenyl)-N-((4-chlorophenyl)sulfonyl)-3-methyl-1H-pyrazole-4-carboxamide
-
5-chloro-1-(4-chlorophenyl)-N-((4-methoxyphenyl)-sulfonyl)-3-methyl-1H-pyrazole-4-carboxamide
73% inhibition at 100 mg/l
5-chloro-1-(4-fluorophenyl)-3-methyl-N-((4-(trifluoromethoxy)phenyl)sulfonyl)-1H-pyrazole-4-carboxamide
-
5-chloro-1-(4-fluorophenyl)-3-methyl-N-(phenylsulfonyl)-1H-pyrazole-4-carboxamide
-
5-chloro-1-(4-fluorophenyl)-3-methyl-N-tosyl-1H-pyrazole-4-carboxamide
-
5-chloro-1-(4-fluorophenyl)-N-((4-methoxyphenyl)-sulfonyl)-3-methyl-1H-pyrazole-4-carboxamide
-
5-chloro-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-chloro-3-methyl-1-(p-tolyl)-N-((4-(trifluoromethoxy)-phenyl)sulfonyl)-1H-pyrazole-4-carboxamide
-
5-chloro-3-methyl-1-(p-tolyl)-N-tosyl-1H-pyrazole-4-carboxamide
-
5-chloro-3-methyl-1-phenyl-N-((4-(trifluoromethoxy)phenyl)-sulfonyl)-1H-pyrazole-4-carboxamide
81% inhibition at 100 mg/l
5-chloro-3-methyl-1-phenyl-N-(phenylsulfonyl)-1H-pyrazole-4-carboxamide
-
5-chloro-3-methyl-1-phenyl-N-tosyl-1H-pyrazole-4-carboxamide
-
5-chloro-3-methyl-N-(phenylsulfonyl)-1-(p-tolyl)-1H-pyrazole-4-carboxamide
-
5-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
-
5-chloro-N-((4-chlorophenyl)sulfonyl)-1-(4-fluorophenyl)-3-methyl-1H-pyrazole-4-carboxamide
-
5-chloro-N-((4-chlorophenyl)sulfonyl)-3-methyl-1-(p-tolyl)-1H-pyrazole-4-carboxamide
-
5-chloro-N-((4-chlorophenyl)sulfonyl)-3-methyl-1-phenyl-1H-pyrazole-4-carboxamide
65% inhibition at 100 mg/l
5-chloro-N-((4-methoxyphenyl)sulfonyl)-3-methyl-1-(p-tolyl)-1H-pyrazole-4-carboxamide
-
5-chloro-N-((4-methoxyphenyl)sulfonyl)-3-methyl-1-phenyl-1H-pyrazole-4-carboxamide
-
5-cyano-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
inhibition profile and inhibition of root growth, overview
8-(4,6-dimethoxypyrimidin-2-yloxy)-4-methylphthalazin-1(2H)-one
-
-
8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
Ag+
-
0.1 mM, 98% residual activity
bensulfuron-methyl
a sulfonylurea herbicide; mutant W548L/S627I, 22% inhibition at 0.1 nM
benzaldehyde
-
inhibits isozyme AHAS II, not isozyme AHAS I
branched-chain amino acids
-
feedback inhibition, differential inhibition of isozymes, overview
-
chlorimuron-ethyl
-
binding conformation
chlorimuronethyl
-
noncompetitive, lowest total interaction energy and highest MolDock score of 140054 kcal/mol and -141.52, respectively, of the compounds analyzed
Co2+
-
0.1 mM, 44% residual activity
ethyl 2-([(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate
-
compound binds within a pocket of the enzyme formed by amino acid residues Met351, Asp375, Arg377, Gly509, Met570 and Val571
ethyl 2-([(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate
-
compound binds within a pocket of the enzyme formed by amino acid residues Met351, Asp375, Arg377, Gly509, Met570 and Val571
ethyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
ethyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
ethyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
ethyl 2-[(pyrimidin-2-ylcarbamoyl)sulfamoyl]benzoate
-
-
ethyl 2-[([4-[(acryloyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)sulfamoyl]benzoate
-
-
ethyl 2-[[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4-chloro-6-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 2-[[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
ethyl 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methyl[1,1'-biphenyl]-2-carboxylate
-
ethyl 4-chloro-2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
FAD
-
0.01 mM, 92% inhibition
glyoxylate
-
isozyme AHAS II
Hg2+
-
0.1 mM, 43% residual activity
Hydroxypyruvate
-
progressive inactivation of enzyme with kinetics of suicide inhibition, mechanism
KIH-6127
-
i.e. pyriminobac-methyl
L-2-aminobutanoate
-
5 mM, 21% inhibition
L-Thr
-
5 mM, 6.6% inhibition
methyl 2-([(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate
-
methyl 2-([[4-(ethylsulfanyl)-6-methoxypyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-(methylamino)-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-chloro-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-chloro-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
-
-
methyl 2-[[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
methyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
methyl 2-[[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
-
methyl 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylate
-
methyl 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylate
-
methyl-2-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoylsulfamoyl]benzoate
-
Mg2+
-
0.5 mM, 80% residual activity
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
N-([4-[(benzyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)-2-chlorobenzenesulfonamide
-
-
N-([5-bromo-4-[(prop-2-en-1-yloxy)methyl]pyrimidin-2-yl]carbamoyl)-2-(2-chloroethoxy)benzenesulfonamide
-
-
N-phenyl-3-(phenyldisulfanyl)-1H-1,2,4-triazole-1-carboxamide
strong inhibition
N-phthalyl-L-isoleucine anilide
50% inhibition at 0.1 mM, crude enzyme preparation
N-phthalyl-L-phenylalanine anilide
50% inhibition at 0.047 mM, crude enzyme preparation
N-phthalyl-L-valine anilide
50% inhibition at 0.0023 mM, crude enzyme preparation
N-phthalyl-L-valine-anilide
-
and related compounds
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-(ethylsulfanyl)-6-(2-fluoro-1-hydroxyethyl)benzenesulfonamide
-
i.e. K12147
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-fluoro-6-nitrobenzenesulfonamide
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-iodo-6-nitrobenzenesulfonamide
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitro-6-(2,2,2-trifluoroethoxy)benzenesulfonamide
N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[(5-bromo-4-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[(5-bromopyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
N-[[5-bromo-4-(1-methylethoxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(ethenyloxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
-
-
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
-
-
N-[[5-bromo-4-(tribromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
-
-
NADP+
-
0.01 mM, 63% inhibition
NADPH
-
0.01 mM, 100% inhibition
phosphate
-
inhibits activity of enzyme assayed in acetate buffer
phosphoenolpyruvate
-
noncompetitive
primisulfuron methyl
-
IC50: 0.0042 mM, over 80% inhibition at 0.04 mM
primisulfuron-methyl
-
1 mM, 50% inhibition
propan-2-yl 4-bromo-3-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
-
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
pyrazosulfuron-ethyl
a sulfonylurea herbicide
pyrimidinyl-(thio) benzoates
pyrimidinylthiobenzoate
-
pyrimidylsalicylate
-
0.025 mM, 60% inhibition
pyriminobac
a pyrimidinylcarboxylate herbicide; mutant W548L/S627I, 13% inhibition at 0.1 nM
pyriminobac-methyl
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 9.2fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
pyrithiobac sodium
inhibitor of wild-type enzyme, poor inhibition of the P197E mutant enzyme
pyrithiobac-sodium
a pyrimidinylcarboxylate herbicide; mutant W548L/S627I, 32% inhibition at 0.1 nM
SO42-
-
competitive when assayed in phosphate buffer, mixed type, when assayed in acetate buffer
sodium 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylate
-
sodium 3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylate
-
sulfonylaminocarbonyltriazolinone
-
thiamine thiazolone diphosphate
-
-
thifensulfuron-methyl
-
-
triasulfuron
-
21 out of 27 isolated bacteria in pure culture are inhibited by triasulfuron, the addition of isoleucine and/or valine reverses the effect in 19 cases
tribenuron
inhibitor of wild-type enzyme, poor inhibition of the P197E mutant enzyme
triflusulfuron methyl
-
1 mM, 50% inhibition
[1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
[5-bromo-2-[([[2-(1-methoxyethenyl)phenyl]sulfonyl]carbamoyl)amino]pyrimidin-4-yl]methyl prop-2-enoate
-
-
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, 50% inhibition at 0.00318 mM, mutant C411S, 50% inhibition at 0.00426 mM, mutant C607S, 50% inhibition at 0.00099 mM
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
i.e. Cadre
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
-
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
i.e. Cadre
2-bromo-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
67.5% inhibition at 10 mg/l
2-bromo-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
68.9% inhibition at 10 mg/l
2-bromo-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
64.8% inhibition at 10 mg/l
2-bromo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-bromo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
69.9% inhibition at 10 mg/l
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
68.2% inhibition at 10 mg/l
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
62.2% inhibition at 10 mg/l
2-chloro-N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
64.1% inhibition at 10 mg/l
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
62.2% inhibition at 10 mg/l
2-chloro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
67.7% inhibition at 10 mg/l
2-chloro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-chloro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
44.5% inhibition at 10 mg/l
2-fluoro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
67.9% inhibition at 10 mg/l
2-fluoro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
72.6% inhibition at 10 mg/l
2-fluoro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-fluoro-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
68.9% inhibition at 10 mg/l
2-iodo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
68.5% inhibition at 10 mg/l
2-iodo-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-iodo-N-[(4-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
-
2-oxobutanoate
-
isoenzyme I has lower sensitivity to inhibition than isoenzyme III
2-oxobutanoate
-
inhibits formation of acetolactate from pyruvate
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
-
bensulfuron
-
bispyribac
-
bispyribac
about 58% enzyme inhibition after 2 h at enzyme:inhibitor ratio of 10:1
bispyribac-sodium
-
bispyribac-sodium
almost no effect on the mutant W548L/S627I even at 100 mM, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type; a pyrimidinylcarboxylate herbicide
bispyribac-sodium
a pyrimidinyl carboxy herbicide
Cadre
-
an imidazolinone herbicide
Cadre
-
an imidazole herbicide, no inhibition of mutant R372S/F373P/D374V/D375E/R376Y
Cadre
-
an imidazole herbicide, wild-type enzyme IC50: 0.0041 mM
Cadre
-
imidazolinone inhibitor
chlorimuron ethyl
-
a sulfonylurea herbicide, complex inhibition, binding structure, overview
chlorimuron ethyl
about 90% enzyme inhibition after 2 h at enzyme:inhibitor ratio of 10:1
chlorimuron ethyl
-
a sulfonylurea herbicide, complex inhibition, overview
chlorimuron ethyl
-
a sulfonylurea herbicide
chlorimuron ethyl
a sulfonylurea herbicide, complex inhibition, overview
chlorimuron ethyl
-
a sulfonylurea herbicide, complex inhibition, overview
chlorimuron ethyl
-
IC50: 0.009 mM, over 80% inhibition at 0.04 mM
chlorimuron ethyl
a sulfonylurea derivative herbicide
chlorimuron ethyl
-
a sulfonylurea herbicide, complex inhibition, overview
chlorsulfuron
-
-
chlorsulfuron
a sulfonylurea herbicide
chlorsulphuron
-
-
chlorsulphuron
-
inhibition of the enzyme from Arabidopsis thaliana and of the enzyme expressed in E. coli
EDTA
-
dialysis against EDTA leads to an irreversible loss of activity
EDTA
-
20 mM, no residual activity
florasulam
-
florasulam
inhibitor of wild-type enzyme, poor inhibition of the P197E mutant enzyme
flucarbazone
-
flumetsulam
-
-
flumetsulam
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 6.5fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
foramsulfuron
-
Ile
-
insensitive to
Ile
-
mild inhibition of isoenzyme I and III
Ile
-
isoenzyme AHS I is sensitive to feed-back inhibition, isoenzyme AHS II is insensitive
Ile
-
5 mM, 32% inhibition
Ile
-
inhibition of isoenzyme I, no inhibition of isoenzyme II
Ile
-
less potent, noncompetitive
Ile
-
1 mM, 50% inhibition
Ile
-
enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited
imazamox
-
imazapyr
-
-
imazapyr
-
an imidazolinone herbicide, complex inhibition, overview
imazapyr
-
an imidazolinone herbicide, complex inhibition, overview
imazapyr
-
an imidazolinone herbicide
imazapyr
an imidazolinone herbicide, complex inhibition, overview
imazapyr
-
an imidazolinone herbicide, complex inhibition, overview
imazapyr
-
i.e. 2-(4-isopropyl-4-methyl-5-oxo-2-imidazolin-2-yl)nicotinic acid
imazapyr
-
a imidazolinone herbicide, complex inhibition, overview
imazapyr
an imidazolinon herbicide; mutant W548L/S627I, 27% inhibition at 0.1 nM
imazapyr
-
enzyme form AHS I and AHS II
imazapyr
-
slow, tight-binding inhibitor
imazaquin
-
an imidazolinone herbicide, complex inhibition, binding structure, overview
imazaquin
about 20% enzyme inhibition after 2 h at enzyme:inhibitor ratio of 10:1, about 85% enzyme inhibition after 2 days at enzyme:inhibitor ratio of 1000:1
imazaquin
-
uncompetitive
imazaquin
-
an imidazolinone herbicide, complex inhibition, overview
imazaquin
an imidazolinone herbicide, complex inhibition, overview
imazaquin
-
an imidazolinone herbicide, complex inhibition, overview
imazaquin
-
a imidazolinone herbicide, complex inhibition, overview
imazaquin
an imidazolinon herbicide
imazaquin
-
1 mM, 50% inhibition
imazethapyr
-
imazethapyr
inhibitor of wild-type enzyme, poor inhibition of the P197E mutant enzyme
imazethapyr
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 12.6fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
imazosulfuron
a sulfonylurea herbicide
imazosulfuron
-
sulfonylurea-resistant biotype, 50% inhibition above 3000 nM, sulfonylurea-susceptible biotype, 50% inhibition at 15 nM
imazosulfuron
60-80% inhibition at 0.1-100 mM imazosulfuron; no or poor inhibition of resistant mutant enzyme, IC50 values in different plant accessions, overview; no or poor inhibition of resistant mutant enzyme, IC50 values in different plant accessions, overview
imidazolinone
-
imidazolinones
-
the imidazolinones behave as non-competitive or uncompetitive inhibitors
isoleucine
-
feedback inhibition of wild-type enzyme about 50% at 10 mM, M8 and M13 mutants are resistant
isoleucine
feedback inhibition; feedback inhibition; feedback inhibition
isoleucine
feedback inhibition
isoleucine
-
feedback inhibition
isoleucine
-
feedback inhibition
isoleucine
-
feedback inhibition
isoleucine
-
1 mM, about 90% residual activity in both sulfonylurea-susceptible and sulfonylurea-resistant biotype
isoniazid
-
-
K12147
-
-
K13010
-
-
K13030
-
-
KHG20612
-
KHG20612
-
inhibition kinetics and antimycobacterial activity, overview
KHG20612
strong inhibition
L-isoleucine
-
-
L-leucine
-
-
L-valine
-
-
L-valine
-
inhibits to a maximal activity of approximately 50% at concentrations higher than 0.5 mM
L-valine
-
not inhibitory for catalytic subunit alone, inhibitory for catalytic subunit plus small subunit
L-valine
50% inhibition at 20 mM, crude enzyme preparation
Leu
-
insensitive to
Leu
-
inhibition of the enzyme from Arabidopsis thaliana, no inhibition of the enzyme expressed in E. coli
Leu
-
mixed noncompetitive inhibition of isoenzyme, pH-independent inhibition of isoenzyme III
Leu
-
no inhibition of isoenzyme I and III
Leu
-
isoenzyme AHS I is sensitive to feed-back inhibition, isoenzyme AHS II is insensitive
Leu
-
5 mM, 23% inhibition
Leu
-
inhibition of isoenzyme I, no inhibition of isoenzyme II
Leu
-
1 mM, 50% inhibition
Leu
-
enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited
Leu
-
cooperative effect with Val
leucine
-
feedback inhibition
leucine
-
feedback inhibition
leucine
-
feedback inhibition of wild-type enzyme about 50% at 10 mM, M8 and M13 mutants are resistant
leucine
-
feedback inhibition
leucine
feedback inhibition; feedback inhibition; feedback inhibition
leucine
feedback inhibition
leucine
-
feedback inhibition
leucine
feedback inhibition
leucine
-
feedback inhibition
leucine
-
feedback inhibition
leucine
-
feedback inhibition
leucine
feedback inhibition
leucine
-
feedback inhibition
leucine
-
feedback inhibition
leucine
-
1 mM, about 50% residual activity in both sulfonylurea-susceptible and sulfonylurea-resistant biotype
leucine
-
feedback inhibition
Londax
-
a sulfonylurea herbicide
Londax
-
a sulfonylurea herbicide, no inhibition of mutant R372S/F373P/D374V/D375E/R376Y
Londax
-
a sulfonylurea herbicide, wild-type enzyme IC50: 0.013 mM
mesosulfuron
-
metosulam
-
metsulfuron methyl
-
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron methyl
-
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron methyl
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron methyl
-
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron methyl
-
IC50: 0.006 mM, over 80% inhibition at 0.04 mM
metsulfuron methyl
-
a sulfonylurea herbicide, complex inhibition, overview
metsulfuron-methyl
-
-
metsulfuron-methyl
herbicide-resistant enzyme variant from Pseudomonas sp. Lm10 shows 56fold higher resistance than the sensitive variant from Pseudomonas putida KT2440
Mn2+
-
0.5 mM, 28% residual activity
Mn2+
-
activates, high concentrations inhibit
monosulfuron
-
-
monosulfuron
93% inhibition at 100 mg/l
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
wild-type, 50% inhibition at 0.00262 mM, mutant C411S, 50% inhibition at 0.00668 mM, mutant C607S, 50% inhibition at 0.00887 mM
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
i.e. TP
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-fluoro-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-fluoro-6-nitrobenzenesulfonamide
-
68.4% inhibition at 10 mg/l
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-fluoro-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-fluoro-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-fluoro-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-iodo-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-iodo-6-nitrobenzenesulfonamide
-
65.1% inhibition at 10 mg/l
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-iodo-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-iodo-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-iodo-6-nitrobenzenesulfonamide
-
-
N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitro-6-(2,2,2-trifluoroethoxy)benzenesulfonamide
-
-
N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitro-6-(2,2,2-trifluoroethoxy)benzenesulfonamide
-
65.1% inhibition at 10 mg/l
N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitro-6-(2,2,2-trifluoroethoxy)benzenesulfonamide
-
-
N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitro-6-(2,2,2-trifluoroethoxy)benzenesulfonamide
-
-
N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitro-6-(2,2,2-trifluoroethoxy)benzenesulfonamide
-
-
N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
-
-
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
ratio 1:1, i.e. Londax
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
ratio 1:1
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
ratio 1:1, i.e. Londax
NC-311
-
NC-311
-
sulfonylurea derivative, wild-type, 50% inhibition at 9.39 nM, mutant C411S, 50% inhibition at 16.83 nM, mutant C607S, 50% inhibition at 20.25 nM
NC-311
-
sulfonylurea inhibitor
nicosulfuron
-
PCMB
-
-
penoxsulam
-
penoxsulam
95% inhibition after 40 min at 0.002 mM
primisulfuron
-
propoxycarbazone
-
propoxycarbazone
about 55% enzyme inhibition after 2 h at enzyme:inhibitor ratio of 10:1
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e. ZJ0273. Moderate susceptibility of plants
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e.ZJ0273
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e. ZJ0273. ALS activity in vivo is hardly affected by ZJ0273 at 100 mg/l
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
-
i.e. ZJ0273. Decline of ALS activity and lower biomass production at a rate of 10 mg/l of ZJ0273
propyl 4-(2-(4,6-dimethoxypyrimidin-2-yloxy)benzylamino)benzoate
Malachium aquaticum
-
i.e. ZJ0273. Moderate susceptibility of plants
prosulfuron
-
pyrazosulfuron ethyl
-
-
pyrazosulfuron ethyl
-
IC50: 87 nM, over 80% inhibition at 0.04 mM
pyrazosulfuron ethyl
-
IC50: 870 nM
pyriftalid
-
-
pyrimidinyl-(thio) benzoates
-
pyrimidinyl-(thio) benzoates
-
pyrithiobac
-
pyrithiobac
about 70% enzyme inhibition after 2 h at enzyme:inhibitor ratio of 10:1
pyroxsulam
-
pyroxsulam
inhibitor of wild-type enzyme, poor inhibition of the P197E mutant enzyme
rifampicin
-
-
sucrose
-
-
sulfometuron methyl
-
-
sulfometuron methyl
-
the enzyme inhibitor shows activity against Mycobacterium tuberculosis both in vitro and in vivo
sulfometuron methyl
-
the enzyme inhibitor shows activity against Mycobacterium tuberculosis both in vitro and in vivo
sulfometuron methyl
-
IC50: 0.0048 mM, over 80% inhibition at 0.04 mM
sulfometuron methyl
-
active against Mycobacterium tuberculosis both in vitro and in vivo
sulfometuron methyl
-
the enzyme inhibitor shows activity against Mycobacterium tuberculosis both in vitro and in vivo
sulfometuron-methyl
-
-
sulfometuron-methyl
-
2.5 mM, 50% inhibition
sulfometuron-methyl
-
enzyme form AHS I and AHS II
sulfonylurea
-
the inhibition by sulfonylurea is non-competitive or nearly competitive with respect to pyruvate
sulfonylurea
-
potently inhibiting herbicide
thiencarbazone
-
thiencarbazone methyl
-
thiencarbazone methyl
about 40% enzyme inhibition after 2 h at enzyme:inhibitor ratio of 10:1
thiencarbazone methyl
-
-
thiencarbazone methyl
94% inhibition after 60 min at 0.002 mM
tribenuron methyl
-
-
tribenuron-methyl
-
-
trifloxysulfuron
-
tritosulfuron
-
Val
-
no inhibition
Val
-
inhibition of the enzyme from Arabidopsis thaliana, no inhibition of the enzyme expressed in E. coli
Val
-
competitive; feed-back inhibition
Val
-
isoenzymes I and II are inhibited, isoenzyme II is not inhibited
Val
-
isoenzyme I and III inhibited
Val
-
isoenzyme I is more resistant to inhibition than isoenzyme III
Val
-
isoenzyme AHS I is sensitive to feed-back inhibition, isoenzyme AHS II is insensitive
Val
-
5 mM, 89% inhibition; feed-back inhibition; noncompetitive
Val
-
feed-back inhibition
Val
-
feed-back inhibition
Val
-
feed-back inhibition
Val
-
noncompetitive; pH-dependent inhibition
Val
-
isoenzymes I and II are inhibited, isoenzyme II is not inhibited
Val
-
two enzyme forms: one is very sensitive to inhibition by Val, the second is not subject to feedback inhibition
Val
-
feed-back inhibition; noncompetitive
Val
-
0.1 mM, 50% inhibition
Val
-
feed-back inhibition; noncompetitive
Val
-
enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited
Val
-
cooperative effective with Leu
valine
-
feedback inhibition
valine
-
feedback inhibition
valine
-
feedback inhibition of wild-type enzyme about 50% at 10 mM, M8 and M13 mutants are resistant
valine
-
isozyme AHAS I, feedback inhibition
valine
-
isozyme AHAS I, cooperative feedback inhibition
valine
-
binding site structure, inhibition mechanism
valine
-
feedback inhibition
valine
feedback inhibition; feedback inhibition; feedback inhibition
valine
feedback inhibition
valine
-
feedback inhibition
valine
feedback inhibition
valine
-
feedback inhibition
valine
-
feedback inhibition
valine
-
feedback inhibition
valine
-
feedback inhibition, reversible by MgATP2-
valine
feedback inhibition, the inhibition by valine is uniquely in fungi reversed by MgATP
valine
-
feedback inhibition
valine
-
feedback inhibition
valine
-
1 mM, about 70%% residual activity in sulfonylurea-susceptible and 80% in sulfonylurea-resistant biotype
valine
-
feedback inhibition
[1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
a triazolopyrimidine derivative herbicide, no inhibition of mutant R372S/F373P/D374V/D375E/R376Y
[1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
a triazolopyrimidine derivative herbicide, wild-type enzyme IC50: 0.0293 mM
additional information
-
ligand binding structures, and inhibition mechanism, overview
-
additional information
-
AHAS from Bacillus anthracis shows strong resistance to three classes of herbicides, the sulfonylurea Londax, the imidazolinone Cadre, and the triazolopyrimidine TP
-
additional information
-
ligand binding structures, and inhibition mechanism, overview
-
additional information
-
computational database screening for non-sulfonylurea inhibitors of AHAS, overview
-
additional information
-
inhibition kinetics or recombinant wild.type and reconstituted isozymes AHAS I
-
additional information
-
isozyme AHAS II is not feedback inhibited
-
additional information
-
inhibitor synthesis, overview. Determination of ligand-receptor interaction and resistance mechanism in AHAS-sulfonylurea herbicide system, molecular modeling, overview
-
additional information
-
bulky substitutions in ortho-position of the sulfamoyl group in N-[(4-chloropyrimidin-2-yl)carbamoyl]benzenesulfonamide may enhance inhibitory activity. Negative charge distributed over a large surface area may enhance this activity. For better activity, the number of electronegative atoms present in the molecule should be high
-
additional information
feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern
-
additional information
feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern
-
additional information
feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern; feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme. Certain imidazolinones show significant activity against the bacterial enzyme with Ki values of below 0.11 mM. Molecular docking of benzoyl ester compounds. AHAS-inhibitors and the probable binding pattern
-
additional information
ligand binding structures, and inhibition mechanism, overview
-
additional information
inhibitor library screening
-
additional information
-
inhibitor library screening
-
additional information
-
leucine had negligible effect on the activity
-
additional information
-
ligand binding structures, and inhibition mechanism, overview
-
additional information
-
no effect: Mg2+
-
additional information
-
no effect: Mn2+, Mg2+, Ca2+
-
additional information
-
screening of 100 sulfonylurea analogues for antimycobacterial activity, minimal inhibitory concentrations, overview
-
additional information
-
screening of 100 sulfonylurea analogues for antimycobacterial activity, minimal inhibitory concentrations, overview
-
additional information
-
mechanism and potency of enzyme inhibition by sulfonylurea herbicides, overview
-
additional information
-
screening of chemical libraries for effective inhibitors of the enzyme, overview
-
additional information
-
screening of 100 sulfonylurea analogues for antimycobacterial activity, minimal inhibitory concentrations, overview
-
additional information
-
not inhibited by bensulfuron methyl
-
additional information
not inhibited by bensulfuron methyl
-
additional information
-
single stranded DNA aptamers Apt1 (CGAGTGAGGGCGAGGCGCGCTCCTGCCGGT) and Apt6 (CGGCCAGGGGACGAGCGCGCCCTGATCGTG) demonstrate the greatest inhibitory potential against the enzyme activity with IC50 values in the low nanomolar range (28.94 and 22.35 nM respectively). Aptamers Apt2, Apt3 and Apt4 show moderate to lower inhibition specificities
-
additional information
-
screening of 100 sulfonylurea analogues for antimycobacterial activity, minimal inhibitory concentrations, overview
-
additional information
-
enzyme mutation P197E causes chick weed plant resistance to ALS inhibitors in population WRR04
-
additional information
enzyme mutation P197E causes chick weed plant resistance to ALS inhibitors in population WRR04
-
additional information
-
IC50 values of herbicides with mutant enzymes, overview
-
additional information
-
ligand binding structures, and inhibition mechanism, overview
-
additional information
-
feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme
-
additional information
molecular docking of inhibitor molecules to the enzyme crystal structure, 3D-QSAR modeling, overview
-
additional information
-
feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme
-
additional information
-
feedback inhibition takes place in the holoenzyme containing the regulatory and the catalytic subunits. The branched-chain amino acids are believed to bind only to the regulatory subunit and inhibit the enzyme
-
additional information
-
the majority of soil bacteria contain only one functional acetohydroxyacid synthase enzyme sensitive to sulfonylurea herbicides
-
additional information
no inhibition by N-phthalyl-L-leucine, N-phthalyl-L-norleucine, N-phthalyl-L-phenylglycine, N-phthalyl-L-norvaline, N-phthalyl-L-glycine, N-phthalyl-L-alanine, crude enzyme preparation
-
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0.28
thiamine diphosphate
-
-
additional information
additional information
-
1
2-oxobutanoate
-
at 1.5 mM pyruvate
1.37
2-oxobutanoate
-
pH 7.5, 37°C
5
2-oxobutanoate
-
at 2 mM pyruvate
5.6
2-oxobutanoate
-
wild-type, pH 7.3, 37°C
6.9
2-oxobutanoate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C
9.1
2-oxobutanoate
-
mutant V375A, pH 7.6, 37°C
300
2-oxobutanoate
-
wild-type, pH 7.6, 37°C
0.0028
pyruvate
wild type enzyme, at pH 7.5 and 37°C
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged mutant H84A
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged mutant H84T
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged mutant Q86A
0.0028
pyruvate
pH 7.5, 37°C, recombinant His6-tagged wild-type enzyme
0.0117
pyruvate
-
wild-type enzyme
0.0289
pyruvate
-
mutant R372S/F373P/D374V/D375E
0.0757
pyruvate
-
mutant R372S/F373P/D374V/D375E/R376Y
0.141
pyruvate
mutant enzyme Q86A, at pH 7.5 and 37°C
0.15
pyruvate
mutant enzyme H84A, at pH 7.5 and 37°C
0.213
pyruvate
mutant enzyme H84T, at pH 7.5 and 37°C
0.33
pyruvate
-
mutant C83T, pH 7.6, 37°C
1
pyruvate
-
pH 7.6, isoenzyme AHAS I
1.08
pyruvate
mutant F147R, pH 7.5, 37°C
1.09
pyruvate
-
mutant enzyme W574L, at pH 7.5 and 37°C
1.1
pyruvate
mutant Q487S, pH 7.0, 37°C
1.18
pyruvate
wild-type, pH 7.5, 37°C
1.19
pyruvate
-
mutant enzyme P197T, at pH 7.5 and 37°C
1.2
pyruvate
-
mutant C83S, pH 7.6, 37°C
1.3
pyruvate
-
isoenzyme I
1.37
pyruvate
pH 7.5, 37°C, recombinant wild-type enzyme
1.37
pyruvate
pH 6.8, 37°C, recombinant enzyme
1.37
pyruvate
at pH 6.8 and 37°C
1.37
pyruvate
-
wild type enzyme, pH and temperature not specified in the publication
1.37
pyruvate
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
1.37
pyruvate
wild type enzyme, at pH 6.8 and 37°C
1.37
pyruvate
-
mutant enzyme P197L, at pH 7.5 and 37°C
1.38
pyruvate
-
mutant S539R, pH not specified in the publication, temperature not specified in the publication
1.38
pyruvate
-
mutant enzyme P197H, at pH 7.5 and 37°C
1.46
pyruvate
-
mutant enzyme P197S, at pH 7.5 and 37°C
1.5
pyruvate
-
mutant C83A, pH 7.6, 37°C
1.5 - 2
pyruvate
-
mutant enzyme D376E, at pH 7.5 and 37°C
1.56
pyruvate
-
pH 7.0, 37°C, holoenzyme
1.6
pyruvate
mutant Q487G, pH 7.0, 37°C
1.7
pyruvate
-
recombinant mutant E49D, pH and temperature not specified in the publication
1.7
pyruvate
-
mutant enzyme E49D, pH and temperature not specified in the publication
1.74
pyruvate
-
wild type enzyme, at pH 7.5 and 37°C
1.89
pyruvate
mutant L141A, pH 7.5, 37°C
2.2
pyruvate
-
pH 7.0, 30°C, sulfonylurea-resistant biotype
2.49
pyruvate
wild-type, pH 7.5, 37°C
2.6
pyruvate
-
native protein
2.76
pyruvate
-
catalytic subunit
2.76
pyruvate
pH 7.5, 37°C, recombinant wild-type enzyme
2.76
pyruvate
-
pH 7.0, 37°C, catalytic subunit
2.76
pyruvate
wild type enzyme, at pH 7.5 and 37°C
2.9
pyruvate
-
fusion protein containing an N-terminal oligohistidine sequence on the large subunit
3.33
pyruvate
-
mutant S539A, pH not specified in the publication, temperature not specified in the publication
3.35
pyruvate
mutant L89A, pH 7.5, 37°C
3.36
pyruvate
-
mutant S167A, pH not specified in the publication, temperature not specified in the publication
3.6
pyruvate
-
mutant D375E, pH 7.5, 37°C
3.6
pyruvate
-
mutant L476M/Q480W, pH 7.6, 37°C
3.66
pyruvate
-
pH 7.5, 37°C
3.7
pyruvate
-
pH 7.0, 30°C, sulfonylurea-susceptible biotype
3.89
pyruvate
mutant F147A, pH 7.5, 37°C
3.96
pyruvate
-
at pH 6.5 and 37°C
4
pyruvate
-
37°C, reconstituted, recombinant holoenzyme
4.15
pyruvate
-
pH 7.6, 37°C
4.34
pyruvate
pH 7.5, 37°C, recombinant mutant Q411N
4.34
pyruvate
mutant enzyme Q411N, at pH 6.8 and 37°C
4.58
pyruvate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
4.7
pyruvate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C
4.7
pyruvate
-
mutant Q480W, pH 7.6, 37°C
4.8
pyruvate
-
wild-type, pH 7.6, 37°C
4.8
pyruvate
-
pH 7.4, 37°C, recombinant enzyme
4.8
pyruvate
-
37°C, recombinant holoenzyme
4.94
pyruvate
mutant W516R, pH 7.5, 37°C
5
pyruvate
-
wild-type, 37°C, pH 7.6
5.2
pyruvate
-
wild-type, pH 7.6, 37°C
5.7
pyruvate
-
mutant D374A, pH 7.5, 37°C
5.8
pyruvate
mutant R101A, pH 7.5, 37°C
6
pyruvate
-
wild-type with His-tag, pH 7.6, 37°C
6.04
pyruvate
pH 7.5, 37°c, recombinant mutant P126A
6.04
pyruvate
mutant enzyme P126A, at pH 7.5 and 37°C
6.53
pyruvate
-
pH 7.5, 37°C, recombinant wild-type enzyme
6.6
pyruvate
-
wild-type, pH 7.6, 37°C
7
pyruvate
-
enzyme form II
7
pyruvate
-
pH 7.6, isoenzyme AHAS III
7
pyruvate
-
mutant D428N, 37°C, pH 7.6
7.1
pyruvate
-
mutant E47A, pH 7.6, 37°C
7.3
pyruvate
-
mutant E47Q, 37°C, pH 7.6
7.3
pyruvate
-
mutant V375I, pH 7.6, 37°C
7.6
pyruvate
-
isoenzyme III
7.7
pyruvate
-
mutant E47A, 37°C, pH 7.6
7.7
pyruvate
-
mutant E47Q, pH 7.6, 37°C
7.8
pyruvate
-
wild-type, pH 7.3, 37°C
7.82
pyruvate
-
mutant S539F, pH not specified in the publication, temperature not specified in the publication
8
pyruvate
-
enzyme form I
8
pyruvate
-
30°C, 120 ng protein in assay
8
pyruvate
-
mutant V477I, pH 7.6, 37°C
8.01
pyruvate
-
Km-value of the first active site
8.36
pyruvate
-
mutant S506R, pH not specified in the publication, temperature not specified in the publication
8.5
pyruvate
wild type enzyme, at pH 7.5 and 20°C
8.7
pyruvate
mutant Q487A, pH 7.0, 37°C
8.8
pyruvate
holoenzyme, pH 8.0, 60°C
8.8
pyruvate
mutant enzyme S627N, at pH 7.5 and 20°C
8.9
pyruvate
mutant S27A, pH 7.5, 37°C
9
pyruvate
mutant enzyme S627N, in the presence of imazamox, at pH 7.5 and 20°C
9.2
pyruvate
pH 7.5, 37°C, recombinant enzyme
10
pyruvate
-
30°C, 60 ng protein in assay
10
pyruvate
-
pH 7.0, 37°C, isoform ALS I
10.54
pyruvate
-
mutant S506A, pH not specified in the publication, temperature not specified in the publication
10.6
pyruvate
-
pH 7.6, isoenzyme AHAS II
11
pyruvate
-
pH 7.0, 37°C, isoform ALS II
11.2
pyruvate
-
mutant W464L with His-tag, pH 7.6, 37°C
11.4
pyruvate
mutant enzyme S627N, in the presence of imazethapyr, at pH 7.5 and 20°C
11.48
pyruvate
-
mutant S167R, pH not specified in the publication, temperature not specified in the publication
11.7
pyruvate
-
wild-type, pH 7.5, 37°C
11.7
pyruvate
-
pH 7.5, wild-type enzyme
11.9
pyruvate
pH 7.5, 37°C
12
pyruvate
large subunit, pH 8.0, 60°C
12.1
pyruvate
-
wild-type recombinant enzyme
13
pyruvate
-
mutant L476M, pH 7.6, 37°C
13.6
pyruvate
wild-type, pH 7.0, 37°C
13.68
pyruvate
-
mutant C607S, pH 7.5, 37°C
13.71
pyruvate
-
mutant H392M, 37°C, pH 7.5
13.8
pyruvate
-
mutant V375A, pH 7.6, 37°C
14.68
pyruvate
pH 7.5, 37°C, recombinant mutant Q112N
14.68
pyruvate
mutant enzyme Q112N, at pH 6.8 and 37°C
15.05
pyruvate
-
wild-type, pH 7.5, 37°C
16.09
pyruvate
-
wild-type, 37°C, pH 7.5
16.24
pyruvate
-
recombinant mutant E49Q, pH and temperature not specified in the publication
16.24
pyruvate
-
mutant enzyme E49Q, pH and temperature not specified in the publication
16.4
pyruvate
pH 7.0, 80°C
16.4
pyruvate
pH 7.0, 85°C, recombinant catalytic subunit
16.4
pyruvate
at pH 7.0 and 80°C
16.43
pyruvate
pH 7.5, 37°C, recombinant mutant Q411E
16.43
pyruvate
mutant enzyme Q411E, at pH 6.8 and 37°C
17.06
pyruvate
-
wild-type, pH 7.5, 37°C
17.3
pyruvate
-
mutant F109M, pH 7.6, 37°C
17.5
pyruvate
pH 7.5, 37°C
17.9
pyruvate
-
mutant V391A, pH 7.6, 37°C
19.78
pyruvate
pH 7.5, 37°C, recombinant mutant Q112E
19.78
pyruvate
mutant enzyme Q112E, at pH 6.8 and 37°C
21
pyruvate
-
mutant E60Q, pH 7.6, 37°C
21.55
pyruvate
-
mutant C411S, pH 7.5, 37°C
24.6
pyruvate
pH 7.5, 37°C, recombinant mutant H111R
24.6
pyruvate
mutant enzyme H111R, at pH 6.8 and 37°C
25.5
pyruvate
-
pH 7.5, 37°C, in the presence of 3.5 M KCl
26
pyruvate
-
mutant M263A, pH 7.6, 37°C
26.23
pyruvate
-
mutant K299Q pH 7.5, 37°C
28
pyruvate
-
mutant E60A, pH 7.6, 37°C
29.5
pyruvate
-
mutant Q110N, pH 7.6, 37°C
30.2
pyruvate
-
mutant Q110A, pH 7.6, 37°C
30.58
pyruvate
-
recombinant mutant E49A, pH and temperature not specified in the publication
30.58
pyruvate
-
mutant enzyme E49A, pH and temperature not specified in the publication
31.2
pyruvate
pH 7.5, 37°C, recombinant mutant Q112V
31.2
pyruvate
mutant enzyme Q112V, at pH 6.8 and 37°C
36
pyruvate
-
mutant D428E, 37°C, pH 7.6
36
pyruvate
-
mutant M250A with His-tag, pH 7.6, 37°C
36.6
pyruvate
pH 7.5, 37°C, recombinant mutant H111F
36.6
pyruvate
mutant enzyme H111F, at pH 6.8 and 37°C
38
pyruvate
-
mutant R276K with His-tag, pH 7.6, 37°C
40.4
pyruvate
-
mutant Q110H pH 7.6, 37°C
50
pyruvate
-
wild-type, pH 7.3, 37°C, presence of 10 mM L-valine
50
pyruvate
-
mutant R289K, pH 7.6, 37°C
54
pyruvate
-
wild-type, pH 7.3, 37°C, presence of 10 mM L-isoleucine
55.8
pyruvate
-
mutant D374A/D375A, pH 7.5, 37°C
65
pyruvate
-
wild-type, pH 7.3, 37°C, presence of 10 mM L-leucine
70
pyruvate
-
pH 6.5, 37°C
76.63
pyruvate
-
mutantH351F, 37°C, pH 7.5
100
pyruvate
-
Km-value of the second active site
104
pyruvate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-isoleucine
104
pyruvate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-leucine
104
pyruvate
-
mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-valine
109.3
pyruvate
-
mutant D375A, pH 7.5, 37°C
109.4
pyruvate
-
mutant K255F, pH 7.5, 37°C
110.6
pyruvate
-
mutant Q110E, pH 7.6, 37°C
113.9
pyruvate
-
pH 7.5, mutant R141K
115.5
pyruvate
-
mutant K255Q, pH 7.5, 37°C
116.8
pyruvate
-
pH 7.5, mutant R141F
124
pyruvate
-
mutant R289Q, pH 7.6, 37°C
148
pyruvate
-
pH 7.5, 37°C, recombinant mutant W573F
167.4
pyruvate
-
pH 7.5, mutant R372F
266.7
pyruvate
-
mutant D374E/D375E, pH 7.5, 37°C
287.8
pyruvate
-
mutant H351M, 37°C, pH 7.5
337.3
pyruvate
-
pH 7.5, mutant R376K
466.7
pyruvate
pH 7.5, 37°c, recombinant mutant P126V
466.7
pyruvate
mutant enzyme P126V, at pH 7.5 and 37°C
475.9
pyruvate
-
pH 7.5, mutant R372K
557.6
pyruvate
-
mutant D374E, pH 7.5, 37°C
807.7
pyruvate
pH 7.5, 37°c, recombinant mutant P126T
807.7
pyruvate
mutant enzyme P126T, at pH 7.5 and 37°C
959.5
pyruvate
-
mutant H351Q, 37°C, pH 7.5
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
non-hyperbolic substrate-saturation curve, involving interaction between the active sites of the dimer
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of isozymes
-
additional information
additional information
-
cofactor affinities of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics or recombinant wild-type and reconstituted isozymes AHAS I, exclusive binding model
-
additional information
additional information
-
steady-state kinetics at different reaction conditions
-
additional information
additional information
-
steady-state kinetics of recombinant wild-type and mutant enzymes, cofactor binding parameters, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetic analysis, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetic analysis, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetic analysis, overview
-
additional information
additional information
binding kinetics of Mg2+ and thiamine diphosphate with wild-type enzyme and mutant enzymes, overview
-
additional information
additional information
-
binding kinetics of Mg2+ and thiamine diphosphate with wild-type enzyme and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics and optimal reaction conditions, overview
-
additional information
additional information
-
Michaelis-Menten kinetics and optimal reaction conditions, overview
-
additional information
additional information
-
substrate and cofactor kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM)
-
additional information
additional information
activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM)
-
additional information
additional information
activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM)
-
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0.0421
(2E)-3,3'-dioxo-1,1',3,3'-tetrahydro-2,2'-biindole-5,5'-disulfonate
-
pH 7.0, 37°C
0.00291
2'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.0757 - 0.0929
2-(2,3-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.0158 - 0.228
2-(2,3-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00212 - 0.00758
2-(2,4-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.0147 - 0.0843
2-(2,4-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.0144 - 0.0553
2-(2,5-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00572 - 0.0263
2-(2,5-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00458 - 0.047
2-(2-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
3.62
2-(2-bromobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
0.0257 - 0.0657
2-(2-bromophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00159 - 0.0037
2-(2-chloro-4-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
2.1
2-(2-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
0.00827 - 0.212
2-(2-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00694 - 0.145
2-(3-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
2.16
2-(3-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
0.00184 - 0.0434
2-(3-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00141 - 0.00334
2-(4-bromo-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.0157 - 0.0189
2-(4-chloro-2-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00325 - 0.00916
2-(4-chloro-2-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00134 - 0.00642
2-(4-chloro-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
2.03
2-(4-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
0.00451 - 0.056
2-(4-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00452
2-(5-chloropyridin-3-yl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylbenzoic acid
pH and temperature not specified in the publication
0.00000939 - 0.181
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
0.00989
2-(6-chloropyridin-3-yl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylbenzoic acid
pH and temperature not specified in the publication
0.0000153
2-bromo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
apparent value, pH and temperature not specified in the publication
6.47
2-bromopyruvate
-
pH 7.5, 37°C
4.41
2-butyl-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
0.0001729
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
apparent value, pH and temperature not specified in the publication
0.0000115
2-fluoro-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
apparent value, pH and temperature not specified in the publication
0.0000229
2-iodo-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]-6-nitrobenzenesulfonamide
-
apparent value, pH and temperature not specified in the publication
0.00053 - 0.00335
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-3-methylphenoxy)benzoic acid
0.00607 - 0.0202
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-4-methylphenoxy)benzoic acid
0.00537 - 0.0612
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-5-methylphenoxy)benzoic acid
0.0274 - 0.108
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluorophenoxy)benzoic acid
0.00201 - 0.0605
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-fluorophenoxy)benzoic acid
0.00645 - 0.0201
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-methylphenoxy)benzoic acid
0.0119 - 0.0214
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-fluorophenoxy)benzoic acid
0.0178 - 0.0234
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-methylphenoxy)benzoic acid
0.00179 - 0.00317
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(naphthalen-2-yloxy)benzoic acid
0.0042 - 0.0528
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-phenoxybenzoic acid
0.0498
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(5-methylpyridin-3-yl)benzoic acid
pH and temperature not specified in the publication
0.00025
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(naphthalen-2-yl)benzoic acid
pH and temperature not specified in the publication
0.00531
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(pyridin-3-yl)benzoic acid
pH and temperature not specified in the publication
0.705
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methyl-6-(pyrimidin-5-yl)benzoic acid
pH and temperature not specified in the publication
0.0597
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(2-methoxypyrimidin-5-yl)-4-methylbenzoic acid
pH and temperature not specified in the publication
0.00378
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(3,5-dimethyl-1,2-oxazol-4-yl)-4-methylbenzoic acid
pH and temperature not specified in the publication
0.0309
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(6-fluoropyridin-3-yl)-4-methylbenzoic acid
pH and temperature not specified in the publication
0.00066
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(furan-2-yl)-4-methylbenzoic acid
pH and temperature not specified in the publication
0.00051
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(furan-3-yl)-4-methylbenzoic acid
pH and temperature not specified in the publication
0.00271 - 0.00369
2-[([1,1'-biphenyl]-4-yl)oxy]-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
0.00403
3'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.0907
3-(7H-cyclopenta[b]pyridin-5-yl)-N-[(2-nitrophenyl)sulfanyl]alanine
-
pH 7.0, 37°C
0.00207
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-2'-fluoro-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00728
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3',5'-difluoro-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00215
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3'-fluoro-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00018
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4',5-dimethylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00067
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4'-fluoro-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00154
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4'-methoxy-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.663
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.0268
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00273
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methyl-4'-nitrobiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00009
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00002
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.00041
4'-bromo-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.0391
4'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
0.0002
4'-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbiphenyl-2-carboxylic acid
pH and temperature not specified in the publication
1
5-chloro-3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
IC50 above 1.0 mM, pH and temperature not specified in the publication
0.0152
6,6'-disulfanediyldipyridine-3-carboxylic acid
-
pH 7.0, 37°C
0.789
8-(4,6-dimethoxypyrimidin-2-yloxy)-4-methylphthalazin-1(2H)-one
-
-
7.89
8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
1.4
benzaldehyde
-
isozyme AHAS II
0.0000409 - 0.00247
bispyribac
0.000011 - 0.0000747
chlorimuron ethyl
0.0000524
chlorsulfuron
-
apparent value, pH and temperature not specified in the publication
0.00038 - 0.036
flumetsulam
0.121
imazethapyr
pH 7.5, 37°C
0.19
L-isoleucine
-
at pH 6.5 and 37°C
0.0119
L-leucine
-
at pH 6.5 and 37°C
0.201
metsulfuron-methyl
pH 7.5, 37°C
0.00000045 - 0.79
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
0.0000283
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-fluoro-6-nitrobenzenesulfonamide
-
apparent value, pH and temperature not specified in the publication
0.0001127
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-iodo-6-nitrobenzenesulfonamide
-
apparent value, pH and temperature not specified in the publication
0.0001658
N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitro-6-(2,2,2-trifluoroethoxy)benzenesulfonamide
-
apparent value, pH and temperature not specified in the publication
0.00000823 - 0.00086
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
0.00000939 - 0.0000202
NC-311
1
primisulfuron-methyl
-
-
0.000179
propoxycarbazone
at pH 7.2 and 30°C
0.065
pyriminobac-methyl
pH 7.5, 37°C
0.0004348
pyrithiobac
at pH 7.2 and 30°C
0.0003 - 0.041
sulfometuron methyl
2.5
sulfometuron-methyl
-
-
0.0006708
thiencarbazone methyl
at pH 7.2 and 30°C
0.00008 - 0.212
tribenuron-methyl
1
triflusulfuron methyl
-
-
additional information
leucine/valine
0.0757
2-(2,3-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0929
2-(2,3-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0158
2-(2,3-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.228
2-(2,3-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00212
2-(2,4-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.00758
2-(2,4-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0147
2-(2,4-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0843
2-(2,4-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0144
2-(2,5-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0553
2-(2,5-dichlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00572
2-(2,5-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0263
2-(2,5-difluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00458
2-(2-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.047
2-(2-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0257
2-(2-bromophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0657
2-(2-bromophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00159
2-(2-chloro-4-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0037
2-(2-chloro-4-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00827
2-(2-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.212
2-(2-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00694
2-(3-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.145
2-(3-bromo-4-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00184
2-(3-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0434
2-(3-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00141
2-(4-bromo-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.00334
2-(4-bromo-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0157
2-(4-chloro-2-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0189
2-(4-chloro-2-fluorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00325
2-(4-chloro-2-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.00916
2-(4-chloro-2-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00134
2-(4-chloro-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.00642
2-(4-chloro-3-methylphenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00451
2-(4-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.056
2-(4-chlorophenoxy)-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00000939
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, pH 7.5, 37°C
0.0000168
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant C411S, pH 7.5, 37°C
0.0000202
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant C607S, pH 7.5, 37°C
0.0008
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D375A, pH 7.5, 37°C
0.00109
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant K299Q pH 7.5, 37°C
0.00122
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, pH 7.5, 37°C
0.00135
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, 37°C, pH 7.5
0.00205
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant H392M, 37°C, pH 7.5
0.0041
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
wild-type, pH 7.5, 37°C
0.0133
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374A/D375A, pH 7.5, 37°C
0.0155
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374E, pH 7.5, 37°C
0.01735
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutantH351F, 37°C, pH 7.5
0.0296
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374E/D375E, pH 7.5, 37°C
0.0389
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D375E, pH 7.5, 37°C
0.181
2-(5-ethyl-3-methylpyridin-2-yl)-5-isopropyl-5-methyl-3,5-dihydro-4H-imidazol-4-one
-
mutant D374A, pH 7.5, 37°C
0.00053
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-3-methylphenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.00335
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-3-methylphenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00607
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-4-methylphenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0202
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-4-methylphenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00537
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-5-methylphenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0612
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluoro-5-methylphenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0274
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluorophenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.108
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(2-fluorophenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00201
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-fluorophenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0605
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-fluorophenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00645
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-methylphenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0201
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(3-methylphenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0119
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-fluorophenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0214
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-fluorophenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0178
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-methylphenoxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0234
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(4-methylphenoxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00179
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(naphthalen-2-yloxy)benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.00317
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-(naphthalen-2-yloxy)benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.0042
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-phenoxybenzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0528
2-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]-6-phenoxybenzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00271
2-[([1,1'-biphenyl]-4-yl)oxy]-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.00369
2-[([1,1'-biphenyl]-4-yl)oxy]-6-[(4,6-dimethoxy-1,3,5-triazin-2-yl)oxy]benzoic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.0000409
bispyribac
at pH 7.2 and 30°C
0.000054
bispyribac
-
wild type enzyme, pH and temperature not specified in the publication
0.00054
bispyribac
pH and temperature not specified in the publication
0.00247
bispyribac
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.000011
chlorimuron ethyl
-
about
0.0000747
chlorimuron ethyl
at pH 7.2 and 30°C
0.00038
flumetsulam
pH and temperature not specified in the publication
0.036
flumetsulam
pH 7.5, 37°C
0.0000185
imazaquin
at pH 7.2 and 30°C
0.00273
L-valine
-
at pH 6.5 and 37°C
0.105
L-valine
pH 7.5, 37°C
0.16
L-valine
-
catalytic subunit plus small subunit, pH 7.0, 30°C
0.00000045
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutantH351F, 37°C, pH 7.5
0.00000311
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
wild-type, 37°C, pH 7.5
0.00000365
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant H392M, 37°C, pH 7.5
0.00000368
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant H351M, 37°C, pH 7.5
0.00000939
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
wild-type, pH 7.5, 37°C
0.0000168
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant C411S, pH 7.5, 37°C
0.0000202
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant C607S, pH 7.5, 37°C
0.00004857
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant H351Q, 37°C, pH 7.5
0.00301
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant K299Q pH 7.5, 37°C
0.00527
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
wild-type, pH 7.5, 37°C
0.0293
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
wild-type, pH 7.5, 37°C
0.036
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant D374E, pH 7.5, 37°C
0.0741
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant D374A, pH 7.5, 37°C
0.198
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant D375A, pH 7.5, 37°C
0.309
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant D374A/D375A, pH 7.5, 37°C
0.79
N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
-
mutant D374E/D375E, pH 7.5, 37°C
0.00000823
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
wild-type, pH 7.5, 37°C
0.00000902
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant K299Q pH 7.5, 37°C
0.0000093
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant H392M, 37°C, pH 7.5
0.0000109
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
wild-type, 37°C, pH 7.5
0.000013
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
wild-type, pH 7.5, 37°C
0.00002304
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutantH351F, 37°C, pH 7.5
0.000108
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant D374E, pH 7.5, 37°C
0.00086
N-[[(4-methoxy-1,3,5-triazin-2-yl)amino]carbonyl]-1-phenylmethanesulfonamide - methyl hydroperoxide
-
mutant D374A, pH 7.5, 37°C
0.00000939
NC-311
-
wild-type, pH 7.5, 37°C
0.0000168
NC-311
-
mutant C411S, pH 7.5, 37°C
0.0000202
NC-311
-
mutant C607S, pH 7.5, 37°C
0.0003
sulfometuron methyl
-
mutant E47Q, 37°C, pH 7.6
0.0006
sulfometuron methyl
-
mutant E47A, 37°C, pH 7.6
0.0008
sulfometuron methyl
-
wild-type, 37°C, pH 7.6
0.0032
sulfometuron methyl
-
mutant D428N, 37°C, pH 7.6
0.0044
sulfometuron methyl
-
mutant Q480W, pH 7.6, 37°C
0.005
sulfometuron methyl
-
pH 7.5, 37°C, in the presence of 3.5 M KCl
0.006
sulfometuron methyl
-
mutant D428E, 37°C, pH 7.6
0.012
sulfometuron methyl
holoenzyme, pH 7.9, 55°C
0.041
sulfometuron methyl
-
mutant L476M/Q480W, pH 7.6, 37°C
0.00008
tribenuron-methyl
-
wild type enzyme, pH and temperature not specified in the publication
0.212
tribenuron-methyl
-
mutant enzyme P197L, pH and temperature not specified in the publication
0.003
valine
-
pH 7.0, 30°C, mutant L222A
0.006
valine
-
pH 7.0, 30°C, mutant K218A
0.0156
valine
-
pH 7.0, 30°C, mutant S212A
0.0162
valine
-
pH 7.0, 30°C, mutant L177A
0.018
valine
holoenzyme, pH 8.0, 60°C
0.02
valine
-
pH 7.0, 30°C, mutant H205A
0.0245
valine
-
pH 7.0, 30°C, mutant R216A
0.026
valine
-
pH 7.0, 30°C, mutant F204A
0.039
valine
-
pH 7.0, 30°C, mutant P206A
0.058
valine
-
pH 7.0, 30°C, mutant H181A
0.177
valine
-
pH 7.0, 30°C, wild-type enzyme
16.3
valine
-
pH 7.0, 37°C, holoenzyme
additional information
leucine/valine
-
an equimolar mixture of leucine and valine
additional information
additional information
-
-
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics of sulfonylurea herbicides
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.006
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00484
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl phenylacetate
Escherichia coli
-
pH 7.5, 22°C
0.00584
(5-bromo-2-[[([2-[(2-chloroethoxy)methyl]phenyl]sulfonyl)carbamoyl]amino]pyrimidin-4-yl)methyl prop-2-enoate
Escherichia coli
-
pH 7.5, 22°C
0.021
1-(4,6-dimethoxypyrimidin-2-yl)-5-methoxymethyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
Escherichia coli
-
pH 7.6, 37°C
0.022
1-(4,6-dimethoxypyrimidin-2-yl)-5-methyl-N-(2-isopropyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
Escherichia coli
-
pH 7.6, 37°C
0.032
1-(4,6-dimethoxypyrimidin-2-yl)-5-methylthio-N-(2-chloro-6-fluorophenyl)-1H-1,2,4-triazole-3-sulfonamide
Escherichia coli
-
pH 7.6, 37°C
0.03
1-(4-chloro-6-methoxypyrimidin-2-yl)-5-methoxy-N-(2-methyl-6-nitrophenyl)-1H-1,2,4-triazole-3-sulfonamide
Escherichia coli
-
pH 7.6, 37°C
0.00603
2,3-dichloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00568
2-(1,1-dihydroxyethyl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00746
2-(2-chloroethoxy)-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00452
2-(2-chloroethoxy)-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.1
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-(trifluoromethyl)benzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-chlorobenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.0065
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-fluorobenzoate
Mycobacterium tuberculosis
-
at pH 7.5 and 37°C
0.1
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl 3-methoxybenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
2-(3-fluorophenyl)-4-oxoquinazolin-3(4H)-yl benzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00957
2-(3-methoxyphenyl)-4-oxoquinazolin-3(4H)-yl 3-(trifluoromethyl)benzoate
Mycobacterium tuberculosis
-
at pH 7.5 and 37°C
0.1
2-(3-methoxyphenyl)-4-oxoquinazolin-3(4H)-yl 3-chlorobenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00874
2-(3-methoxyphenyl)-4-oxoquinazolin-3(4H)-yl 3-nitrobenzoate
Mycobacterium tuberculosis
-
at pH 7.5 and 37°C
0.00719
2-(difluoromethoxy)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00684
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00714
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.007
2-amino-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00782
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.0074
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.00621
2-butoxy-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00267
2-chloro-3-oxocyclohex-1-en-1-yl 3-(trifluoromethyl)benzoate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0141
2-chloro-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00178
2-chloro-6-(methoxycarbonyl)-5,5-dimethyl-3-oxocyclohex-1-en-1-yl 4-chlorobenzoate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00762
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00749
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.00529
2-chloro-N-([4-(methylamino)-6-[(1-methylethyl)sulfanyl]-1,3,5-triazin-2-yl]carbamoyl)benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00693
2-chloro-N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00471
2-chloro-N-[(4,6-dimethylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00649
2-chloro-N-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00541
2-chloro-N-[[4-(ethylsulfanyl)-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00369
2-chloro-N-[[4-(ethylsulfanyl)-6-methoxy-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00442
2-chloro-N-[[4-(ethylsulfanyl)-6-methylpyrimidin-2-yl]carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00525
2-chloro-N-[[4-(methylamino)-6-(methylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00556
2-chloro-N-[[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00355
2-chloro-N-[[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00352
2-chloro-N-[[4-methyl-6-(propylsulfanyl)pyrimidin-2-yl]carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00202
2-phenyl-3-[[3-(trifluoromethyl)benzoyl]oxy]quinazolin-4(3H)-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00531
2-[(2-chloroethoxy)methyl]-N-[(4-chloropyrimidin-2-yl)carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00533
2-[(2-chloroethoxy)methyl]-N-[(4-methylpyrimidin-2-yl)carbamoyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00633
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.00539
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-methylbenzoic acid
Saccharomyces cerevisiae
-
0.00432
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-(methylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00459
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethylbenzoic acid
Saccharomyces cerevisiae
-
0.0047
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethynylbenzoic acid
Saccharomyces cerevisiae
-
0.00627
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.0072
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-hydroxybenzoic acid
Saccharomyces cerevisiae
-
0.00505
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-iodobenzoic acid
Saccharomyces cerevisiae
-
0.0046
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybenzoic acid
Saccharomyces cerevisiae
-
0.00503
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbenzoic acid
Saccharomyces cerevisiae
-
0.0039
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-nitrobenzoic acid
Saccharomyces cerevisiae
-
0.00573
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1-methylethoxy)benzoic acid
Saccharomyces cerevisiae
-
0.00828
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1H-pyrrol-1-yl)benzoic acid
Saccharomyces cerevisiae
-
0.00711
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(ethylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00757
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00587
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfonyl)benzoic acid
Saccharomyces cerevisiae
-
0.00567
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(phenylcarbonyl)benzoic acid
Saccharomyces cerevisiae
-
0.00629
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(propylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00696
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(trifluoromethoxy)benzoic acid
Saccharomyces cerevisiae
-
0.00705
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethoxybenzoic acid
Saccharomyces cerevisiae
-
0.00657
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethylbenzoic acid
Saccharomyces cerevisiae
-
0.0073
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.00766
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-iodobenzoic acid
Saccharomyces cerevisiae
-
0.00736
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methoxybenzoic acid
Saccharomyces cerevisiae
-
0.00689
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methylbenzoic acid
Saccharomyces cerevisiae
-
0.00664
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-nitrobenzoic acid
Saccharomyces cerevisiae
-
0.0077
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-phenoxybenzoic acid
Saccharomyces cerevisiae
-
0.00624
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propoxybenzoic acid
Saccharomyces cerevisiae
-
0.00589
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propylbenzoic acid
Saccharomyces cerevisiae
-
0.00664
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00488
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(1-methylethoxy)benzoic acid
Saccharomyces cerevisiae
-
0.00667
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(ethylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00768
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(methylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00519
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(phenylcarbonyl)benzoic acid
Saccharomyces cerevisiae
-
0.00572
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(propylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00602
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(trifluoromethyl)benzoic acid
Saccharomyces cerevisiae
-
0.0067
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-ethoxybenzoic acid
Saccharomyces cerevisiae
-
0.00767
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.00699
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-iodobenzoic acid
Saccharomyces cerevisiae
-
0.00705
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methoxybenzoic acid
Saccharomyces cerevisiae
-
0.00753
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methylbenzoic acid
Saccharomyces cerevisiae
-
0.00669
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-nitrobenzoic acid
Saccharomyces cerevisiae
-
0.0056
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-phenoxybenzoic acid
Saccharomyces cerevisiae
-
0.00614
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-propoxybenzoic acid
Saccharomyces cerevisiae
-
0.0068
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.00712
2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]-N,N-dimethylbenzamide
Escherichia coli
-
pH 7.5, 22°C
0.00185
3-[(3-bromobenzoyl)oxy]-2-phenylquinazolin-4(3H)-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0078
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
Saccharomyces cerevisiae
-
0.01413
3-[(4-nitrobenzoyl)oxy]quinazolin-4(3H)-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.1
4-oxo-2-m-tolylquinazolin-3(4H)-yl 3-fluorobenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-m-tolylquinazolin-3(4H)-yl 3-methylbenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-m-tolylquinazolin-3(4H)-yl 4-chlorobenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-m-tolylquinazolin-3(4H)-yl 4-methylbenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-m-tolylquinazolin-3(4H)-yl benzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-m-tolylquinazolin-3(4H)-yl-3-(trifluoromethyl)benzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-o-tolylquinazolin-3(4H)-yl 3-fluorobenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-phenylquinazolin-3(4H)-yl 2-methylbenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.01208
4-oxo-2-phenylquinazolin-3(4H)-yl 3-chlorobenzoate
Mycobacterium tuberculosis
-
at pH 7.5 and 37°C
0.1
4-oxo-2-phenylquinazolin-3(4H)-yl 3-fluorobenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-phenylquinazolin-3(4H)-yl 3-methoxybenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-phenylquinazolin-3(4H)-yl 3-methylbenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00968
4-oxo-2-phenylquinazolin-3(4H)-yl 3-nitrobenzoate
Mycobacterium tuberculosis
-
at pH 7.5 and 37°C
0.1
4-oxo-2-phenylquinazolin-3(4H)-yl 4-chlorobenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-phenylquinazolin-3(4H)-yl 4-methylbenzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.1
4-oxo-2-phenylquinazolin-3(4H)-yl benzoate
Mycobacterium tuberculosis
-
IC50 above 0.1 mM, at pH 7.5 and 37°C
0.00609
5-amino-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00358
5-benzyl-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00571
5-bromo-2-([[(2-chlorophenyl)sulfonyl]carbamoyl]amino)pyrimidin-4-yl benzoate
Escherichia coli
-
pH 7.5, 22°C
0.0045
5-bromo-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00535
5-chloro-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00371
5-cyano-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00053
AVS-2087
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
0.00000000423 - 0.00000423
bensulfuron
0.000007
bensulfuron-methyl
Oryza sativa
wild-type, pH 7.5, 30°C
0.00000000158 - 0.00000158
bispyribac
0.0000056 - 0.000421
bispyribac-sodium
0.00897 - 0.009
chlorimuron ethyl
0.007
chlorimuronethyl
Bacillus anthracis
-
37°C
0.000017 - 0.000093
chlorsulfuron
0.0078
ethyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00651
ethyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.0067
ethyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.0055
ethyl 2-[(pyrimidin-2-ylcarbamoyl)sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00711
ethyl 2-[([4-[(acryloyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.0092
ethyl 2-[[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.0061
ethyl 2-[[(4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00834
ethyl 2-[[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00709
ethyl 2-[[(4-chloro-6-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00669
ethyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00703
ethyl 2-[[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00678
ethyl 2-[[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.0068
ethyl 2-[[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00002
ethyl 5-[(4,6-dimethoxy-2-pyrimidinyl)aminocarbonylaminosulfonyl]-1-methyl-1H-pyrazole-4-carboxylate
Oryza sativa
wild-type, pH 7.5, 30°C
0.00000000343 - 0.00000343
florasulam
0.0000000245 - 0.0000245
flucarbazone
0.0000000075 - 0.0000075
foramsulfuron
0.00000293 - 0.00293
imazamox
0.00000606 - 0.0096
imazapyr
0.00000155 - 0.0167
imazaquin
0.000025 - 0.065
imazosulfuron
0.00177 - 0.00491
KHG20612
0.00142
KSW30191
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
0.012 - 0.32
L-isoleucine
0.0014 - 0.0016
L-leucine
0.00000000133 - 0.00000133
mesosulfuron
0.00458
methyl 2-([[4-(ethylsulfanyl)-6-methoxypyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00733
methyl 2-([[4-(methylamino)-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00686
methyl 2-([[4-chloro-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00631
methyl 2-([[4-chloro-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00786
methyl 2-([[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00646
methyl 2-([[4-methoxy-6-(methylsulfanyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00474
methyl 2-([[4-methoxy-6-(propylsulfanyl)-1,3,5-triazin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00415
methyl 2-([[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00482
methyl 2-([[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00461
methyl 2-([[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00605
methyl 2-([[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]sulfamoyl)benzoate
Escherichia coli
-
pH 7.5, 22°C
0.0071
methyl 2-[[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00571
methyl 2-[[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00453
methyl 2-[[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl]benzoate
Escherichia coli
-
pH 7.5, 22°C
0.00596
methyl-2-[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)carbamoylsulfamoyl]benzoate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000000000441 - 0.000000441
metosulam
0.00596 - 0.006
metsulfuron methyl
0.0046
N-([4-[(benzyloxy)methyl]-5-bromopyrimidin-2-yl]carbamoyl)-2-chlorobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00531
N-([5-bromo-4-[(prop-2-en-1-yloxy)methyl]pyrimidin-2-yl]carbamoyl)-2-(2-chloroethoxy)benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00177
N-phenyl-3-(phenyldisulfanyl)-1H-1,2,4-triazole-1-carboxamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.008
N-[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00769
N-[(4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00523
N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00552
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.0053
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00545
N-[(5-bromo-4,6-dimethoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.0048
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00488
N-[(5-bromo-4,6-dimethylpyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00478
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00477
N-[(5-bromo-4-chloro-6-methoxypyrimidin-2-yl)carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00508
N-[(5-bromo-4-methoxypyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00553
N-[(5-bromo-4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00388
N-[(5-bromopyrimidin-2-yl)carbamoyl]-2-chlorobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.0044
N-[[5-bromo-4-(1-methylethoxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00516
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00669
N-[[5-bromo-4-(bromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00503
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00697
N-[[5-bromo-4-(dibromomethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.0036
N-[[5-bromo-4-(ethenyloxy)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00427
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00514
N-[[5-bromo-4-(ethoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00566
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-chlorobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.00617
N-[[5-bromo-4-(methoxymethyl)pyrimidin-2-yl]carbamoyl]-2-[(2-chloroethoxy)methyl]benzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.0058
N-[[5-bromo-4-(tribromomethyl)pyrimidin-2-yl]carbamoyl]-2-nitrobenzenesulfonamide
Escherichia coli
-
pH 7.5, 22°C
0.0000000714 - 0.0000714
nicosulfuron
0.00000000314 - 0.00000314
primisulfuron
0.0042
primisulfuron methyl
Mycobacterium tuberculosis
-
IC50: 0.0042 mM, over 80% inhibition at 0.04 mM
0.00000000928 - 0.0000928
propoxycarbazone
0.00000000288 - 0.00000288
prosulfuron
0.000087 - 0.00087
pyrazosulfuron ethyl
0.05
pyrazosulfuron-ethyl
Oryza sativa
mutant W548L/S627I, pH 7.5, 30°C
0.000008
pyriminobac
Oryza sativa
wild-type, pH 7.5, 30°C
0.000000000742 - 0.000000742
pyrithiobac
0.000011
pyrithiobac-sodium
Oryza sativa
wild-type, pH 7.5, 30°C
0.00000000412 - 0.00000412
pyroxsulam
0.00479 - 0.2763
sulfometuron methyl
0.01
sulfometuronmethyl
Bacillus anthracis
-
37°C
0.0000000248 - 0.0000248
thiencarbazone
0.0000000059 - 0.0000059
trifloxysulfuron
0.0000000187 - 0.0000187
tritosulfuron
0.0293
[1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
Nicotiana tabacum
-
a triazolopyrimidine derivative herbicide, wild-type enzyme IC50: 0.0293 mM
0.00503
[5-bromo-2-[([[2-(1-methoxyethenyl)phenyl]sulfonyl]carbamoyl)amino]pyrimidin-4-yl]methyl prop-2-enoate
Escherichia coli
-
pH 7.5, 22°C
additional information
additional information
Schoenoplectiella juncoides
-
sensitivity of different varieties of Schoenoplectus juncoides against herbicides, overview
-
0.00000000423
bensulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00000423
bensulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00000000158
bispyribac
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00000158
bispyribac
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.0000056
bispyribac-sodium
Oryza sativa
wild-type, pH 7.5, 30°C
0.00000563
bispyribac-sodium
Oryza sativa
pH 7.5, 30°C, wild-type enzyme, callus
0.000421
bispyribac-sodium
Oryza sativa
mutant W548L/S627I, pH 7.5, 30°C
0.000421
bispyribac-sodium
Oryza sativa
pH 7.5, 30°C, mutant enzyme, callus
0.00024
Cadre
Nicotiana tabacum
-
mutant S167R, pH not specified in the publication, temperature not specified in the publication
0.00089
Cadre
Nicotiana tabacum
-
mutant S506A, pH not specified in the publication, temperature not specified in the publication
0.0026
Cadre
Nicotiana tabacum
-
mutant S167A, pH not specified in the publication, temperature not specified in the publication
0.0035
Cadre
Nicotiana tabacum
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0041
Cadre
Nicotiana tabacum
-
an imidazole herbicide, wild-type enzyme IC50: 0.0041 mM
0.00897
chlorimuron ethyl
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.009
chlorimuron ethyl
Mycobacterium tuberculosis
-
IC50: 0.009 mM, over 80% inhibition at 0.04 mM
0.000017
chlorsulfuron
Oryza sativa
wild-type, pH 7.5, 30°C
0.0000173
chlorsulfuron
Oryza sativa
pH 7.5, 30°C, wild-type enzyme, callus
0.0000928
chlorsulfuron
Oryza sativa
pH 7.5, 30°C, mutant enzyme, callus
0.000093
chlorsulfuron
Oryza sativa
mutant W548L/S627I, pH 7.5, 30°C
0.00000000343
florasulam
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00000343
florasulam
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.0000000245
flucarbazone
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.0000245
flucarbazone
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.0000000075
foramsulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.0000075
foramsulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00000293
imazamox
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00293
imazamox
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00000606
imazapyr
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00606
imazapyr
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.0096
imazapyr
Oryza sativa
wild-type, pH 7.5, 30°C
0.00000155
imazaquin
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00148
imazaquin
Oryza sativa
wild-type, pH 7.5, 30°C
0.00148
imazaquin
Oryza sativa
pH 7.5, 30°C, wild-type enzyme, callus
0.00155
imazaquin
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00697
imazaquin
Bacillus anthracis
-
37°C
0.0167
imazaquin
Oryza sativa
mutant W548L/S627I, pH 7.5, 30°C
0.0167
imazaquin
Oryza sativa
pH 7.5, 30°C, mutant enzyme, callus
0.000025
imazosulfuron
Oryza sativa
wild-type, pH 7.5, 30°C
0.065
imazosulfuron
Oryza sativa
mutant W548L/S627I, pH 7.5, 30°C
0.00177
KHG20612
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00491
KHG20612
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
0.012
L-isoleucine
Mycobacterium tuberculosis
wild-type, pH 7.5, 37°C
0.04
L-isoleucine
Mycobacterium tuberculosis
R101A, pH 7.5, 37°C
0.062
L-isoleucine
Mycobacterium tuberculosis
mutant S27A, pH 7.5, 37°C
0.32
L-isoleucine
Mycobacterium tuberculosis
L89A, pH 7.5, 37°C
0.0014
L-leucine
Mycobacterium tuberculosis
R101A, pH 7.5, 37°C
0.0016
L-leucine
Mycobacterium tuberculosis
wild-type, pH 7.5, 37°C
0.004
L-valine
Mycobacterium tuberculosis
R101A, pH 7.5, 37°C
0.005
L-valine
Mycobacterium tuberculosis
wild-type, pH 7.5, 37°C
0.0075
L-valine
Mycobacterium tuberculosis
mutant S27A, pH 7.5, 37°C
0.012
L-valine
Mycobacterium tuberculosis
L89A, pH 7.5, 37°C
0.00064
Londax
Mycobacterium tuberculosis
wild-type, pH 7.5, 37°C
0.013
Londax
Nicotiana tabacum
-
a sulfonylurea herbicide, wild-type enzyme IC50: 0.013 mM
0.021
Londax
Mycobacterium tuberculosis
mutant L141A, pH 7.5, 37°C
0.00000000133
mesosulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00000133
mesosulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.000000000441
metosulam
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.000000441
metosulam
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00596
metsulfuron methyl
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.006
metsulfuron methyl
Mycobacterium tuberculosis
-
IC50: 0.006 mM, over 80% inhibition at 0.04 mM
0.008
NC-311
Nicotiana tabacum
-
mutant S506A, pH not specified in the publication, temperature not specified in the publication
0.011
NC-311
Mycobacterium tuberculosis
mutant L141A, pH 7.5, 37°C
0.032
NC-311
Nicotiana tabacum
-
mutant S167A, pH not specified in the publication, temperature not specified in the publication
0.048
NC-311
Mycobacterium tuberculosis
wild-type, pH 7.5, 37°C
0.054
NC-311
Nicotiana tabacum
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0000000714
nicosulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.0000714
nicosulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00000000314
primisulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00000314
primisulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00000000928
propoxycarbazone
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.0000928
propoxycarbazone
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00000000288
prosulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00000288
prosulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.000087
pyrazosulfuron ethyl
Mycobacterium tuberculosis
-
IC50: 87 nM, over 80% inhibition at 0.04 mM
0.00087
pyrazosulfuron ethyl
Mycobacterium tuberculosis
-
IC50: 870 nM
0.00002
pyriftalid
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
200
pyriftalid
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.000000000742
pyrithiobac
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.000000742
pyrithiobac
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00000000412
pyroxsulam
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.00000412
pyroxsulam
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.00479
sulfometuron methyl
Mycobacterium tuberculosis
-
at pH 7.5 and 37°C
0.00479
sulfometuron methyl
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0048
sulfometuron methyl
Mycobacterium tuberculosis
-
IC50: 0.0048 mM, over 80% inhibition at 0.04 mM
0.2763
sulfometuron methyl
Haemophilus influenzae
pH 7.5, 37°C, recombinant enzyme
0.0000000248
thiencarbazone
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.0000248
thiencarbazone
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.0000000059
trifloxysulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.0000059
trifloxysulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
0.0000000187
tritosulfuron
Poa annua
wild type enzyme, at 37°C, pH not specified in the publication
0.0000187
tritosulfuron
Arabidopsis thaliana
pH 7.0, 30°C, recombinant wild-type enzyme
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evolution
acetolactate synthase and pyruvate decarboxylase are both thiamine diphosphate-dependent enzymes that use pyruvate as a substrate, but they produce different products.Whereas pyruvate decarboxylase catalyzes the non-oxidative decarboxylation of pyruvate to acetaldehyde, acetolactate synthase, which is involved in the biosynthesis of branched amino acids (Val, Leu, Ile), catalyzes the carboligation between two pyruvate molecules to form an acetolactate molecule and carbon dioxide, structural and functional similarities of the enzymes, overview
evolution
the enzyme belongs to the ALS enzyme family that forms a distinct subgroup of ThDP-dependent enzymes. The ALS subfamily differs significantly in structure and possibly in catalytic mechanism, phylogenetic analysis. The ThDP-dependent enzymes cluster into three distinct sequence groups: acetolactate synthases, acetohydroxyacid synthases, and carboxylases. Eventhough ALS and AHAS catalyze the same reaction, they show different cofactors and domain structure: AHAS family enzymes have both catalytic and regulatory subunits, structure comparisons, overview
evolution
-
three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit
evolution
-
three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit
evolution
three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit
evolution
three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit
evolution
-
two types of ALSs, anabolic acetohydroxyacid synthase (AHAS) and catabolic ALSs (cALS). The anabolic AHAS is primarily found in plants, fungi, and bacteria, is involved in the biosynthesis of branched-chain amino acids, and contains FAD, whereas the cALS is found only in some bacteria and is involved in the butanediol fermentation pathway. Both of the enzymes are thiamine diphosphate-dependent and require a divalent metal ion for catalytic activity. The catabolic ALS can be distinguished from anabolic AHAS by a low optimal pH of about pH 6.0, FAD-independent functionality, a genetic location within the butanediol operon, and lack of a regulatory subunit. In all of the crystal structures of ThDP-dependent enzymes determined to date, with the exception of glyoxylate carbo-ligase (GCL), a highly conerved glutamate residue is found at hydrogen-bonding distance from the N1' atom of the aminopyrimidine ring of the boundThDP and plays a key role in catalysis. In Enterococcus faecalis it is Glu49
evolution
-
the enzyme belongs to the ALS enzyme family that forms a distinct subgroup of ThDP-dependent enzymes. The ALS subfamily differs significantly in structure and possibly in catalytic mechanism, phylogenetic analysis. The ThDP-dependent enzymes cluster into three distinct sequence groups: acetolactate synthases, acetohydroxyacid synthases, and carboxylases. Eventhough ALS and AHAS catalyze the same reaction, they show different cofactors and domain structure: AHAS family enzymes have both catalytic and regulatory subunits, structure comparisons, overview
-
evolution
-
three types of isozymes, AHAS I, II, III, are found in Enterobacteria encoded by ilvBN, ilvGMEDA, ilvIH operons, respectively. Bacterial AHAS consists of a regulatory and a catalytic subunit
-
evolution
-
acetolactate synthase and pyruvate decarboxylase are both thiamine diphosphate-dependent enzymes that use pyruvate as a substrate, but they produce different products.Whereas pyruvate decarboxylase catalyzes the non-oxidative decarboxylation of pyruvate to acetaldehyde, acetolactate synthase, which is involved in the biosynthesis of branched amino acids (Val, Leu, Ile), catalyzes the carboligation between two pyruvate molecules to form an acetolactate molecule and carbon dioxide, structural and functional similarities of the enzymes, overview
-
malfunction
deletion of the als gene abolishes acetoin production. Deletion of gene als in an engineered strain of Pyrococcus furiosus containing an additional pathway for ethanol production significantly improves the yield of ethanol
malfunction
-
enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis
malfunction
-
enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis
malfunction
enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis
malfunction
enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis
malfunction
the A205F substitution in acetolactate synthase, confirmed in a population of allotetraploid annual bluegrass, confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylaminocarbonyl triazolinones, and pyrimidinyl(thio)benzoate herbicides
malfunction
the als defective strain, which is incapable of producing C4 compounds, appears sensitive to pyruvate under acidic conditions rendering it unable to grow. Accordingly, the als-mutant strain shows a simultaneous inability to alkalinize internal and external media
malfunction
the conserved His84 and Gln86 residues lie in the catalytic dimer interface of the enzyme. Mutational analyses of these invariants lead to significant reduction in their activity with reduced affinity toward the substrate
malfunction
the deletion mutants DELTAMoilv2 and DELTAMoilv6 are both auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity, phenotypes, overview
malfunction
the sulfonylurea-resistant plants, found in a population from paddy fields in Japan, harbor amino acid substitutions at Pro197 or Trp574 in either ALS1 or ALS2 (the amino acid number is standardized to the Arabidopsis thaliana sequence)
malfunction
deletion of the enzyme gene abolishes acetoin production
malfunction
-
the enzyme-deficient strain cannot produce acetoin, 2,3-butanediol, and L-valine
malfunction
-
the als defective strain, which is incapable of producing C4 compounds, appears sensitive to pyruvate under acidic conditions rendering it unable to grow. Accordingly, the als-mutant strain shows a simultaneous inability to alkalinize internal and external media
-
malfunction
-
the enzyme-deficient strain cannot produce acetoin, 2,3-butanediol, and L-valine
-
malfunction
-
the conserved His84 and Gln86 residues lie in the catalytic dimer interface of the enzyme. Mutational analyses of these invariants lead to significant reduction in their activity with reduced affinity toward the substrate
-
malfunction
-
enzyme inhibition abolishes biosynthesis of brachend chain amino acids and leads to bacteriostasis
-
malfunction
-
the deletion mutants DELTAMoilv2 and DELTAMoilv6 are both auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity, phenotypes, overview
-
metabolism
acetohydroxyacid synthase is the key enzyme in branched chain amino acid biosynthesis pathway, overview
metabolism
acetohydroxyacid synthase or asacetolactate synthase catalyzes the first step in the biosynthe-sis of branched-chain amino acids such as isoleucine, leucine, and valine. This reaction involves synthesizing either (2S)-acetolactate from two molecules of pyruvate or (2S)-2-aceto-2-hydroxybutyrate from pyruvate and 2-oxobutyrate
metabolism
acetolactate synthase catalyses the first common step in leucine, isoleucine and valine biosynthesis
metabolism
acetolactate synthase is a thiamine diphosphate-dependent enzyme that is involved in the biosynthesis of branched amino acids (Val, Leu, Ile), catalyzing the carboligation between two pyruvate molecules to form an acetolactate molecule and carbon dioxide
metabolism
enzyme AHAS catalyses the condensation of either two molecules of pyruvate to form acetolactate in the leucine and valine pathway, or of one molecule of pyruvate with one molecule of 2-oxobutyrate toform 2-aceto-2-hydroxybutyrate as the first step in the isoleucine biosynthesis
metabolism
-
fermentation pathways in Klebsiella pneumoniae, overview. The biosynthesis route of 2,3-BD in Klebsiella pneumoniae proceeds via pyruvate, acetolactate, and acetoin to 2,3-BD. 2,3-BD production from pyruvate involves three enzymes, namely, 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase (ALDC), and acetoin reductase (AR). These enzymes catalyze the production of acetolactate from pyruvate, acetoin from acetolactate, and 2,3-BD from acetoin
metabolism
key enzyme for the biosynthesis of branched-chain amino acids (valine, leucine and isoleucine) that are required for plant growth
metabolism
strain IL1403 is able to cometabolize pyruvate and glucose at low pH, producing lactate, acetate as well as diacetyl/acetoin compounds. The enzyme is involved in the pyruvate metabolism in Lactococcus lactis, overview
metabolism
the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation
metabolism
-
the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-oxobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation
metabolism
-
the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-oxobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation
metabolism
the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-oxobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation
metabolism
-
the enzyme catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine
metabolism
the enzyme is involved in the branched chain amino acid biosynthesis
metabolism
there are two enzymes in nature that are known to produce 2-acetolactate from pyruvate, a catabolic ALS encoded by the alsSD operon, which is involved in the production of acetoin and butanediol, and ananabolic 2-acetohydroxyacid synthase (AHAS) that participates in biosynthesis of the branched chain amino acids isoleucine, leucine and valine. The flux of 2-acetolactate toward amino acid biosynthesis is regulated via allosteric activation of 2-acetolactate decarboxylase, ALDC, by either valine or leucine
metabolism
isoform Ilv2 plays a crucial role in isoleucine and valine biosynthesis, isoform Ilv6 contributes to isoleucine and leucine biosynthesis
metabolism
-
enzyme overexpression can effectively improve acetoin/2,3-butanediol and L-valine production in Bacillus licheniformis
metabolism
the first enzyme of the biosynthetic pathway that produces the branched-chain of the essential amino acids L-valine, L-leucine, and L-isoleucine
metabolism
-
strain IL1403 is able to cometabolize pyruvate and glucose at low pH, producing lactate, acetate as well as diacetyl/acetoin compounds. The enzyme is involved in the pyruvate metabolism in Lactococcus lactis, overview
-
metabolism
-
fermentation pathways in Klebsiella pneumoniae, overview. The biosynthesis route of 2,3-BD in Klebsiella pneumoniae proceeds via pyruvate, acetolactate, and acetoin to 2,3-BD. 2,3-BD production from pyruvate involves three enzymes, namely, 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase (ALDC), and acetoin reductase (AR). These enzymes catalyze the production of acetolactate from pyruvate, acetoin from acetolactate, and 2,3-BD from acetoin
-
metabolism
-
fermentation pathways in Klebsiella pneumoniae, overview. The biosynthesis route of 2,3-BD in Klebsiella pneumoniae proceeds via pyruvate, acetolactate, and acetoin to 2,3-BD. 2,3-BD production from pyruvate involves three enzymes, namely, 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase (ALDC), and acetoin reductase (AR). These enzymes catalyze the production of acetolactate from pyruvate, acetoin from acetolactate, and 2,3-BD from acetoin
-
metabolism
-
enzyme overexpression can effectively improve acetoin/2,3-butanediol and L-valine production in Bacillus licheniformis
-
metabolism
-
the enzyme is involved in the branched chain amino acid biosynthesis
-
metabolism
-
acetohydroxyacid synthase or asacetolactate synthase catalyzes the first step in the biosynthe-sis of branched-chain amino acids such as isoleucine, leucine, and valine. This reaction involves synthesizing either (2S)-acetolactate from two molecules of pyruvate or (2S)-2-aceto-2-hydroxybutyrate from pyruvate and 2-oxobutyrate
-
metabolism
-
the bacterial anabolic enzyme form catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine. It catalyzes the first and the most crucial step which is either the self condensation of pyruvate to form 2-acetolactate or the condensation between lactate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate. 2-acetolactate and 2-aceto-2-hydroxybutyrate serve as the precursors for the synthesis of leucine and valine while latter serves as the precursor for the synthesis of isoleucine. In some bacteria, the enzyme is responsible for the formation of butanediol and other products of fermentation
-
metabolism
-
isoform Ilv2 plays a crucial role in isoleucine and valine biosynthesis, isoform Ilv6 contributes to isoleucine and leucine biosynthesis
-
metabolism
-
acetolactate synthase catalyses the first common step in leucine, isoleucine and valine biosynthesis
-
metabolism
-
enzyme AHAS catalyses the condensation of either two molecules of pyruvate to form acetolactate in the leucine and valine pathway, or of one molecule of pyruvate with one molecule of 2-oxobutyrate toform 2-aceto-2-hydroxybutyrate as the first step in the isoleucine biosynthesis
-
metabolism
-
acetolactate synthase is a thiamine diphosphate-dependent enzyme that is involved in the biosynthesis of branched amino acids (Val, Leu, Ile), catalyzing the carboligation between two pyruvate molecules to form an acetolactate molecule and carbon dioxide
-
physiological function
-
complete inactivation of the acetolactate synthase in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to improved L-lysine production
physiological function
-
deletion of gene ilv2 encoding acetolactate synthase results in loss of viability during isoleucine and valine starvation due to 2-oxobutanoate accumulation. Rapamycin further decreases vialbility of the mutant. Recovery from starvation is influenced by the carbon source present during recovery
physiological function
-
deletion of gene ilv2 encoding acetolactate synthase results in significant attenuation of virulence and a grater than 100fold reduction in viability after only four hours of isoleucine and valine starvation due to 2-oxobutanoate accumulation. Rapamycin increases vialbility of both ilv1 and ilv2 mutants. Recovery from starvation is influenced by the carbon source present during starvation
physiological function
-
transformation of a H+-ATPase defective strain with a C-terminal truncation of acetohydroxyacid synthase gene ilvBN results in increased valine production from 21.7 mM for wild-type to 46.7 mM and increase in the valine intermediate acetoin. Inserting acetohydroxyacid isomeroreductase gene into the ilvBN plasmid further increases valine producion
physiological function
catabolic acetolactate synthase from Enterococcus faecalis is a FAD-independent enzyme, which catalyzes the condensation of two molecules of pyruvate to produce acetolactate
physiological function
MoIlv2 plays a crucial role in isoleucine and valine biosynthesis, whereas MoIlv6 contributes to isoleucine and leucine biosynthesis, both genes are required for fungal pathogenicity. MoIlv2 and MoIlv6 play a critical role in maintaining the balance of intracellular amino acid levels. And MoIlv2 and MoIlv6 are involved in aerial hyphal growth, pigmentation, conidial morphogenesis and pathogenicity on rice and barley
physiological function
the enzyme is involved in the production of acetoin (3-hydroxybutanone) as a major product at growth temperatures below 80°C. Acetoin is produced by wild-type Pyrococcus furiosus during growth at sub-optimal temperatures below 80°C
physiological function
Pyrococcus furiosus produces acetoin as amajor end product at growth temperatures below 85°C in a temperature-dependent manner via a acetolactate synthase whose gene expression and biochemical function are temperature-dependent
physiological function
the enzyme contributes to pH homeostasis in acid stress conditions
physiological function
the enzyme plays a critical role in maintaining the balance of intracellular amino acid level, is involved in aerial hyphal growth, pigmentation, conidial morphogenesis, and is required for fungal pathogenicity
physiological function
-
the enzyme contributes to pH homeostasis in acid stress conditions
-
physiological function
-
the enzyme plays a critical role in maintaining the balance of intracellular amino acid level, is involved in aerial hyphal growth, pigmentation, conidial morphogenesis, and is required for fungal pathogenicity
-
physiological function
-
MoIlv2 plays a crucial role in isoleucine and valine biosynthesis, whereas MoIlv6 contributes to isoleucine and leucine biosynthesis, both genes are required for fungal pathogenicity. MoIlv2 and MoIlv6 play a critical role in maintaining the balance of intracellular amino acid levels. And MoIlv2 and MoIlv6 are involved in aerial hyphal growth, pigmentation, conidial morphogenesis and pathogenicity on rice and barley
-
additional information
active site structure, catalytically relevant structure-function relationships, overview
additional information
-
active site structure, catalytically relevant structure-function relationships, overview
additional information
homology modeling of Mycobacterium tuberculosis enzyme is performed by using crystal structures, PDB IDs 1N0H and 1JSC, from the Saccharomyces cerevisiae enzyme as template, molcular dynamics simulation
additional information
molecular dynamics simulation studies suggest that the conserved His84 and Gln86 residues residues are likely to play a key role in maintaining the Glu85 side chain in the required geometry with N1'atom of thiamine diphosphate during catalysis
additional information
-
structure homology modeling
additional information
structure homology modeling
additional information
structure homology modeling of wild-type enzyme and H474R enzyme mutant, structure comparisons, overview
additional information
-
structure homology modeling of wild-type enzyme and H474R enzyme mutant, structure comparisons, overview
additional information
the catabolic enzyme form lacks a regulatory subunit. Residue His 111, which is widely present as phenylalanine in many other ThDP-dependent enzymes, plays a crucial role in substrate binding, importance of residues H111, Q112, and Q411 residues for catalysis, Q112 and Q411 might be involved in thiamine diphosphate binding, enzyme structure homology modeling, overview
additional information
-
the catabolic enzyme form lacks a regulatory subunit. Residue His 111, which is widely present as phenylalanine in many other ThDP-dependent enzymes, plays a crucial role in substrate binding, importance of residues H111, Q112, and Q411 residues for catalysis, Q112 and Q411 might be involved in thiamine diphosphate binding, enzyme structure homology modeling, overview
additional information
-
the domains are crucial to the function of MoIlv2 and MoIlv6 during pathogenicity on rice and barley leaves, functional analysis of enzyme domains, overview
additional information
the domains are crucial to the function of MoIlv2 and MoIlv6 during pathogenicity on rice and barley leaves, functional analysis of enzyme domains, overview
additional information
-
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
additional information
-
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
additional information
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
additional information
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
additional information
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
additional information
-
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
additional information
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
additional information
-
wild-type and mutant H28A/N484A active site structure analysis, PDB IDs 2PGN and 4D5G
additional information
-
active site structure, catalytically relevant structure-function relationships, overview
-
additional information
-
wild-type and mutant H28A/N484A active site structure analysis, PDB IDs 2PGN and 4D5G
-
additional information
-
structure homology modeling
-
additional information
-
homology modeling of Mycobacterium tuberculosis enzyme is performed by using crystal structures, PDB IDs 1N0H and 1JSC, from the Saccharomyces cerevisiae enzyme as template, molcular dynamics simulation
-
additional information
-
molecular dynamics simulation studies suggest that the conserved His84 and Gln86 residues residues are likely to play a key role in maintaining the Glu85 side chain in the required geometry with N1'atom of thiamine diphosphate during catalysis
-
additional information
-
there exist two types of the enzyme, catabolic and anabolic AHAS. The anabolic form of the enzyme consists of two subunits out of which one is catalytic while the other is regulatory in nature. The regulatory subunit acts via feedback inhibition
-
additional information
-
the domains are crucial to the function of MoIlv2 and MoIlv6 during pathogenicity on rice and barley leaves, functional analysis of enzyme domains, overview
-
additional information
-
structure homology modeling of wild-type enzyme and H474R enzyme mutant, structure comparisons, overview
-
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multimer
x * 63300, large subunit IlvB, plus x * 18700, small subunit IlvN, SDS-PAGE and calculated.
?
-
x * 59200, calculated from amino acid sequence and SDS-PAGE
?
-
x * 59200, calculated from amino acid sequence and SDS-PAGE
-
?
-
x * 65000, recombinant enzyme, SDS-PAGE
?
-
x * 63000, SDS-PAGE
-
?
x * 60000, recombinant enzyme, SDS-PAGE
?
x * 60200, calculated from amino acid sequence
?
-
x * 9500 + x * 60000, isoenzyme I, SDS-PAGE
?
-
x * 17500 + x * 61800, calculation from nucleotide sequence
?
-
x * 11000 + x * 60000
?
-
x * 16200 + x * 67200, SDS-PAGE
?
x * 63700, recombinant His-tagged catalytic subunit, SDS-PAGE
?
-
x * 58000, SDS-PAGE with urea
?
-
x * 60000, SDS-PAGE
-
?
-
x * 60000, SDS-PAGE
-
?
-
3 major bands detected by SDS-PAGE: 26000 Da, 35000 Da and 46000 Da
?
-
3 major bands detected by SDS-PAGE: 26000 Da, 35000 Da and 46000 Da
-
?
x * 68000, about, wild-type and mutant enzyme variants, SDS-PAGE
?
-
x * 68000, about, wild-type and mutant enzyme variants, SDS-PAGE
-
?
-
x * 68000, SDS-PAGE
-
?
-
x * 48000, deduced from gene sequence
?
x * 64000, mature enzyme, SDS-PAGE
?
x * 62000, SDS-PAGE, catalytic subunit
?
-
x * 62000, SDS-PAGE, catalytic subunit
-
?
-
x * 65000, about, SDS-PAGE and MALDI-TOF spectrometry
?
-
x * 15000 + x * 57000 + x * 58000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 63864, ion spray MS analysis
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
-
2 * 65000 and/or 66000, SDS-PAGE
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
-
2 * 60000, SDS-PAGE
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
-
2 * 64000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
dimer
-
2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
-
dimer
-
the mobile loop comprising residues 567-582 on the C-terminus is involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
-
2 * 75000, SDS-PAGE
dimer
1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
-
2 * 64000, SDS-PAGE
dimer
-
1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
2 * 20508, regulatory subunit, sequence calculation, 2 * 22210, regulatory subunit, SDS-PAGE
dimer
2 * 65497, catalytic subunit, sequence calculation, 2 * 66398, catalytic subunit, SDS-PAGE
dimer
1 * 65497, calculated, 1 * 66400, SDS-PAGE, plus 1 * 2058, calculated, 1 * 22200, SDS-PAGE, catalytic and regulatory subunit, respectively
dimer
-
1 * 65497, calculated, 1 * 66400, SDS-PAGE, plus 1 * 2058, calculated, 1 * 22200, SDS-PAGE, catalytic and regulatory subunit, respectively
-
heterotetramer
2 * 65497 + 2 * 20508, calculated from amino acid sequence
heterotetramer
2 * 66400 + 2 * 22200, SDS-PAGE
homodimer
-
the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer
homodimer
-
the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer
-
homodimer
x-ray crystallography
homotetramer
-
homotetramer
-
in the crystallized form
homotetramer
-
in the crystallized form
-
homotetramer
the enzyme is a homotetramer formed by dimers of dimers, each monomer is composed of three domains. The alpha-domain (up to N181) is connected by a random coil to the central beta-domain (P195 to A346). The C-terminal gamma-domain (from H376) is connected to the central beta-domain by an alpha-helix and a random coil linker, structure-function analysis of the enzyme, overview. The 12 C-terminal resolved residues of AlsS (D556-K567) fold into a short alpha-helix
homotetramer
-
the enzyme is a homotetramer formed by dimers of dimers, each monomer is composed of three domains. The alpha-domain (up to N181) is connected by a random coil to the central beta-domain (P195 to A346). The C-terminal gamma-domain (from H376) is connected to the central beta-domain by an alpha-helix and a random coil linker, structure-function analysis of the enzyme, overview. The 12 C-terminal resolved residues of AlsS (D556-K567) fold into a short alpha-helix
-
monomer
-
1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
monomer
-
1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
-
oligomer
-
x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE
oligomer
-
x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE
-
oligomer
-
8 * 15000 + 8 * 60000, SDS-PAGE
tetramer
the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer
tetramer
-
4 * 65000, SDS-PAGE, both isoforms
tetramer
-
4 * 58000, SDS-PAGE
tetramer
the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer The catalytic subunit has a molecular weight of 60-70 kD, the regulator of 10-45 kD
tetramer
-
the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer The catalytic subunit has a molecular weight of 60-70 kD, the regulator of 10-45 kD
-
tetramer
-
the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer
tetramer
-
2 * 9800 + 2 * 59000, SDS-PAGE
tetramer
-
the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer
trimer
-
3 * 60000, SDS-PAGE
trimer
-
3 * 55000, SDS-PAGE
trimer
-
3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
trimer
-
3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
-
trimer
-
3 * 55000, SDS-PAGE
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
the catabolic enzyme form lacks a regulatory subunit
additional information
-
the catabolic enzyme form lacks a regulatory subunit
additional information
-
enzymes in the AHAS family generally consist of regulatory and catalytic subunits, subunit composition, dimeric structure analysis of the regulatory subunit of isozyme AHAS III, overview
additional information
-
pairs of catalytic subunits form an intimate dimer containing two active sites, each of which lies across a dimer interface and involves both monomers, the catalytic subunit of AHAS II is not active alone
additional information
-
by mapping the 3D contour maps of CoMFA and CoMSIA models into the possible inhibitory active site in the crystal structure of catalytic subunit of yeast AHAS, a plausible binding model for AHAS, with best fit QSAR in the literature so far, is proposed
additional information
-
isozyme AHAS I, catalytic subunit ilvB, regulatory subunit ilvN. AHAS II, catalytic subunit ilvG, regulatory subunit ilvM. Isozyme AHAS III, catalytic subunit ilvI, regulatory subunit ilvH. AHAS II regulatory subunit ilvM is able to activate the catalytic subunits of all three of the isozymes, and the truncated AHAS III regulatory subunits ilvH-DELTA80, ilvH-DELTA86 and ilvH-DELTA89 are able to activate the catalytic subunits of both AHAS I and AHAS III. Contrary to wild-type, none of the heterologously activated enzymes have any feedback sensitivity
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
N-terminal sequence analysis
additional information
-
N-terminal sequence analysis
-
additional information
-
the enzyme consists of two diffrent types of subunits, a catalytic one and a regulatory one
additional information
the enzyme is comprised of two subunits: a large catalytic subunit and asmall regulatory one
additional information
-
the enzyme consists of two diffrent types of subunits, a catalytic one and a regulatory one
-
additional information
-
the enzyme is comprised of two subunits: a large catalytic subunit and asmall regulatory one
-
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the enzyme has a catalytic subunit and a regulatory subunit, encoded by two different genes
additional information
the enzyme has a catalytic subunit and a regulatory subunit, encoded by two different genes
additional information
-
the enzyme has a catalytic subunit and a regulatory subunit, encoded by two different genes
-
additional information
-
heterotetrameric enzyme composed of a small, regulatory and a large, catalytic subunit
additional information
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
-
the enzyme consists of a catalytic and a regulatory subunit
additional information
the enzyme consists of a catalytic and a regulatory subunit
additional information
the enzyme consists of a catalytic and a regulatory subunit
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A205F
site-directed mutagenesis, the enzyme mutation confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylaminocarbonyl triazolinones, and pyrimidinyl(thio)benzoate herbicides
A205V
site-directed mutagenesis
G121A
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
M124E
-
naturally occuring mutation
P197L
-
the mutation causes serious cross-resistance to most types of enzyme inhibitors
R199E
-
naturally occuring mutation
S653F
-
naturally occuring mutation
S653T
-
naturally occuring mutation
H28A
-
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
H28A/N484A
-
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone, e.g. cyclohexane-1,2-dione, in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
H76A
-
site-directed mutagenesis, almost inactive mutant
H76A/Q116A
-
site-directed mutagenesis, inactive mutant
N484A
-
site-directed mutagenesis
Q116A
-
site-directed mutagenesis, inactive mutant
H28A
-
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
-
H28A/N484A
-
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone, e.g. cyclohexane-1,2-dione, in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
-
H76A
-
site-directed mutagenesis, almost inactive mutant
-
Q116A
-
site-directed mutagenesis, inactive mutant
-
K176G
the naturally occuring mutation, substitution of two adenines to guanines in the ilvB gene, causes a cold-sensitive phenotype of mutant strain JH642. The acetolactate synthase efficiency in strain JH642 is reduced by 51fold
K40H
site-directed mutagenesis, the half-life of the mutant at 50°C is 44 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
K40Y
site-directed mutagenesis, the half-life of the mutant at 50°C is 110 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
M483N
site-directed mutagenesis, the mutant is inactivated at 50°C
P87A
site-directed mutagenesis, the half-life of the mutant at 50°C is 33 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
Q124S
site-directed mutagenesis, the half-life of the mutant at 50°C is 42 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
Q424S
site-directed mutagenesis, the half-life of the mutant at 50°C is 104 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows increased activity compared to the wild-type
Q424S/Q487S
site-directed mutagenesis, the half-life of the mutant at 50°C is 94 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
T84V
site-directed mutagenesis, the half-life of the mutant at 50°C is 2.5 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
Y481A
site-directed mutagenesis, the half-life of the mutant at 50°C is 19 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
Q487A
-
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
-
Q487G
-
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
-
Q487I
-
loss of acetolactate synthase activity, decrease in decarboxylase activity
-
Q487L
-
loss of acetolactate synthase activity, decrease in decarboxylase activity
-
Q487S
-
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
-
K40H
-
site-directed mutagenesis, the half-life of the mutant at 50°C is 44 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
-
K40I
-
site-directed mutagenesis, the half-life of the mutant at 50°C is 89 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
-
S638N
-
the mutant is more resistant to imidazolinone herbicides than the wild type in contrast to sulfonylurea herbicides that inhibit the mutant as well as the wild type enzyme
W557L
-
naturally occuring mutation
D376E
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
P197H
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
P197L
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
P197T
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
W574L
-
the resistance mutation causes more than 200fold resistance to tribenuron-methyl and also greatly reduces the enzyme sensitivity to tribenuron-methyl and increases enzyme binding affinity for the substrate pyruvate
A108V
-
naturally occuring mutation
A36V
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
C83A
-
about 91% of wild-type activity
C83S
-
about 126% of wild-type activity
C83T
-
about 41% of wild-type activity
D428E
-
8% activity compared to wild-type
D428N
-
8% activity compared to wild-type
E60A
-
about 48% of wild-type activity
E60Q
-
about 1% of wild-type activity
F109M
-
both substrate affinity and kcat are significantly compromised. The specificity for 2-ketobutyrate as acceptor is not altered
G14A
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
G14D
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
L131R
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
L16A
-
site-directed mutagenesis of the regulatory subunit, the mutant shows increased sensitivity to valine inhibition compared to the wild-type subunit
L476M
-
about 34% of wild-type activity
L476M/Q480W
-
about 47% of wild-type activity
L9A
-
site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit
L9H
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
L9V
-
site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit
M250A
-
large decrease in activity, increase in Km-value
M263A
-
about 16% of wild-type activity
M460N
-
naturally occuring mutation
N11A
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
N11D
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
N11H
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
N29D
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
N29H
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
Q110A
-
about 3% of wild-type activity
Q110E
-
about 1.5% of wild-type activity
Q110H
-
about 15% of wild-type activity
Q110N
-
about 8% of wild-type activity
Q480W
-
about 22% of wild-type activity
R269Q
-
about 0.5% of wild-type activity
R276K
-
large decrease in activity, increase in Km-value
R289K
-
about 11% of wild-type activity
T34C
-
site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit
T34I
-
site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit
T47C
-
site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit
V153D
-
site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine
V35A
-
site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit
V375I
-
slightly reduced kcat value with a moderate increase of the apparent KM of pyruvate. The specificity for 2-ketobutyrate as acceptor is not altered
V391A
-
about 3% of wild-type activity
V477I
-
about 8% of wild-type activity
W464A
-
naturally occuring mutation
W464Q
-
naturally occuring mutation
W464Y
-
naturally occuring mutation
W46F
-
naturally occuring mutation
W563C
naturally occuring mutation
W563S
naturally occuring mutation
A205V
-
naturally occuring mutation
F147A
4fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
F147R
2.5fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
L141A
5fold decrease in vmax value
P126A
site-directed mutagenesis, the mutant exhibits similar kinetics but significantly lower activity compared to the wild-type enzyme
P126A,
the mutant exhibits significantly lower activity than the wild type enzyme
W561R
30fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
E85A
-
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate, , the enzyme shows reduced activity compared to the wild-type enzyme
-
F147A
-
4fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
-
F147R
-
2.5fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
-
L141A
-
5fold decrease in vmax value
-
P126A
-
site-directed mutagenesis, the mutant exhibits similar kinetics but significantly lower activity compared to the wild-type enzyme
-
P126A,
-
the mutant exhibits significantly lower activity than the wild type enzyme
-
W561R
-
30fold decrease in vmax value, strong resistance to sulfonylurea inhibitors
-
A121T
-
naturally occuring mutation
C163S
-
labile, readlily degraded
C309S
-
labile, readlily degraded
C411A
-
no enzymic activity, no binding of FAD
C607S
-
no significant effects
D374A/D375A
-
strong resistance to Londax and to C, about 2fold increase in affinity for FAD, decrease in activation efficiency for thiamine diphosphate
D374E
-
greatly reduced activity, strong resistance to Londax, 8fold increase in affinity for FAD, decrease in activation efficiency for thiamine diphosphate
D374E/D375E
-
strong resistance to Londax and to C
DELTA567
-
deletion of entire C-terminus including mobile loop and C-terminal lid, no enzymic activity
DELTA567-582
-
deletion of mobile loop region 4.5% of activity compared to wild-type, increase in activation constant of thiamine diphosphate
DELTA598
-
deletion of c-terminus maintaining mobile loop and C-terminal lid, 1.2% of activity compared to wild-type
DELTA630
-
deletion of C-terminal lid, 4.5% of activity compared to wild-type, increase in activation constant of thiamine diphosphate
F577D
-
naturally occuring mutation
F577E
-
naturally occuring mutation
H351F
-
5fold increase in Km-value, weak resistance to Londax and Cadre, difference in secondary structure compared to wild-type
H351M
-
18fold increase in Km-value, strong resistance to Londax and Cadre, difference in secondary structure compared to wild-type
H392M
-
no significant effects
H487F
-
no enzymic activity, no affinity for FAD
H487L
-
no enzymic activity, no affinity for FAD
K219Q
-
no residual activity, no binding of FAD
K299Q
-
no significant effects
M350C
-
naturally occuring mutation
M569C
-
naturally occuring mutation
R141A
-
site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD
R141F
-
site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD
R141K
-
site-directed mutagenesis, the mutant shows reduced activity and activation by thiamine diphosphate compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
R372F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
R372K
-
site-directed mutagenesis, the mutant shows reduced activity and activation by FAD compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
R372S/F373P/D374V
-
site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity
R372S/F373P/D374V/D375E
-
site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity
R372S/F373P/D374V/D375E/R376Y
-
site-directed mutagenesis, mutation of the conserved motif 372RFDDR376 results in abolished FAD binding and highly reduced activity, the mutant is resistant to herbocides
R376F
-
site-directed mutagenesis, inactive mutant, unable to bind the cofactor FAD
R376K
-
site-directed mutagenesis, the mutant shows reduced activity and activation by FAD compared to the wild-type enzyme, the mutant is partially resistant to herbicides, e.g. Londax, Cadre, and/or TP
S167A
-
73% of wild-type activity
S167F
-
inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type
S167R
-
250% of wild-type activity
S506A
-
230% of wild-type activity
S506F
-
inactive, mutation abolishes the binding affinity for cofactor FAD. The far-UV spectrum is similar to wild-type
S506R
-
183% of wild-type activity
S539A
-
73% of wild-type activity, strong resistance to herbicides NC-311, a sulfonylurea, Cadre, an imidazolinone, and a triazolopyrimidine
S539F
-
171% of wild-type activity, strong resistance to herbicides NC-311, a sulfonylurea, Cadre, an imidazolinone, and a triazolopyrimidine
S539R
-
30% of wild-type activity
S652T
-
naturally occuring mutation
V570Q
-
naturally occuring mutation
W573F
-
site-directed mutagenesis, the mutant shows 69fold reduced activity compared to the wild-type enzyme, substitution of the W573 residue causes significant perturbations in the activation process and in the binding site of thiamine diphosphate
A96T
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
A96V
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
F180R
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
G95A
the naturally occuring mutation leads to resistance against pyrimidinyl carboxy herbicides, e.g. bispyribac-sodium
M98E
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
M98H
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
M98I
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
P171A
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
P171Q
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
P171S
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
R173A
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
R173E
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627D
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627F
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627N
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627T
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548C
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548F
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548S
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627N
the mutation confers tolerance against imidazolinone herbicides, including imazethapyr and imazamox. The mutant is tolerant to imidazolinone but the catalytic efficiency of the mutated enzyme decreases in its presence. Moreover, the activity of the mutated enzyme decreases more in the presence of imazethapyr than in the presence of imazamox
P197A
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding. Most common mutation among 28 populations resistant to tribenuron
P197L
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
P197R
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
P197S
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
P197T
mutation confers resistance to herbicide tribenuron. Mutation results in altered secondary structure, which stabilizes an ALS tertiary conformation that prevents tribenuron binding
A205V
the mutation confers resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
A117D
naturally occuring mutation
A117E
naturally occuring mutation
A117F
naturally occuring mutation
A117H
naturally occuring mutation
A117I
naturally occuring mutation
A117K
naturally occuring mutation
A117L
naturally occuring mutation
A117M
naturally occuring mutation
A117N
naturally occuring mutation
A117P
naturally occuring mutation
A117Q
naturally occuring mutation
A117R
naturally occuring mutation
A117S
naturally occuring mutation
A117T
naturally occuring mutation
A117V
naturally occuring mutation
A117W
naturally occuring mutation
A117Y
naturally occuring mutation
A200C
naturally occuring mutation
A200D
naturally occuring mutation
A200E
naturally occuring mutation
A200R
naturally occuring mutation
A200T
naturally occuring mutation
A200V
naturally occuring mutation
A200W
naturally occuring mutation
A200Y
naturally occuring mutation
A26V
naturally occuring mutation
D379E
naturally occuring mutation
D379G
naturally occuring mutation
D379N
naturally occuring mutation
D379P
naturally occuring mutation
D379S
naturally occuring mutation
D379V
naturally occuring mutation
D379W
naturally occuring mutation
F204A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
F590C
naturally occuring mutation
F590G
naturally occuring mutation
F590L
naturally occuring mutation
F590N
naturally occuring mutation
F590R
naturally occuring mutation
G116N
naturally occuring mutation
G116S
naturally occuring mutation
H181A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H205A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H219A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
K218A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
K251D
naturally occuring mutation
K251E
naturally occuring mutation
K251N
naturally occuring mutation
K251P
naturally occuring mutation
K251T
naturally occuring mutation
L177A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
L222A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
M354C
naturally occuring mutation
M354K
naturally occuring mutation
M354V
naturally occuring mutation
P192A
naturally occuring mutation
P192E
naturally occuring mutation
P192L
naturally occuring mutation
P192Q
naturally occuring mutation
P192R
naturally occuring mutation
P192S
naturally occuring mutation
P192V
naturally occuring mutation
P192W
naturally occuring mutation
P192Y
naturally occuring mutation
P206A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
R216A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
S212A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
V583A
naturally occuring mutation
V583C
naturally occuring mutation
V583N
naturally occuring mutation
V583Y
naturally occuring mutation
V99M
naturally occuring mutation
W586A
naturally occuring mutation
W586C
naturally occuring mutation
W586E
naturally occuring mutation
W586G
naturally occuring mutation
W586H
naturally occuring mutation
W586I
naturally occuring mutation
W586K
naturally occuring mutation
W586L
naturally occuring mutation
W586N
naturally occuring mutation
W586S
naturally occuring mutation
W586V
naturally occuring mutation
G654D
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
S653I
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
S653N
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
S653T
-
mutant isolated from Ontario population. Mutant confers resistance to herbicide imazethapyr, and cross-resistance to nicosulfuron and flucarbazone
G16D
mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits
G16D/E105stop
no enzymic activity after in vitro reconstitution with large subunit
I106V/A135P
after in vitro reconstitution with large subunit, enzymic activity comparable to wild-type
Q108stop
no enzymic activity after in vitro reconstitution with large subunit
V17D/F30L
no enzymic activity after in vitro reconstitution with large subunit
H747R
mutation leads to 3fold increased acetaldehyde formation, with 30% decrease in acetolactate formation
A122V
-
reduced affinity for all Mg2+, thiamine diphosphate and FAD
A122V
-
naturally occuring mutation
A122V
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
P197S
-
naturally occuring mutation
P197S
Nicotiana tabacum plants with transplastomic expression of mutant are specifically tolerant to pyrimidinylcarboxylate, imidazolinon, and sulfonylurea/pyrimidinylcarboxylate herbicides, respectively
S653N
-
binds FAD more strongly than the wild-type enzyme
S653N
-
naturally occuring mutation
W574L
site-directed mutagenesis
W574L
-
insensitive to sulfonurea herbicides
W574L
-
naturally occuring mutation
W574S
-
reduction in sensitivity to sulfonurea herbicides compared to the wild-type enzyme
W574S
-
naturally occuring mutation
K40I
site-directed mutagenesis, the half-life of the mutant at 50°C is 89 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows highly reduced activity compared to the wild-type
K40I
the mutant shows slightly improved activity towards 2-oxoisovalerate compared to the wild type enzyme
Q487A
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487A
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487G
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487G
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487I
complete loss of synthase activity
Q487I
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487L
complete loss of synthase activity
Q487L
loss of acetolactate synthase activity, decrease in decarboxylase activity
Q487S
mutation diminishes decarboxylase activity but maintains the synthase activity
Q487S
site-directed mutagenesis, the half-life of the mutant at 50°C is 22 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
Q487S
the mutant shows wild type activity towards 2-oxoisovalerate
Q487S
wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity
Q487S
-
site-directed mutagenesis, the half-life of the mutant at 50°C is 22 h, compared to 81 h for the wild-type enzyme, the mutant enzyme shows reduced activity compared to the wild-type
-
Q487S
-
the mutant shows wild type activity towards 2-oxoisovalerate
-
E49A
-
site-directed mutagenesis, the mutant shows decreased activities and weakened thiamine diphosphate binding. The Km for substrate pyruvate is 22fold higher than that of the wild-type cALS. In addition, the E49A mutation also has a drastic effect on cofactor thiamine diphosphate activation. The half-saturating concentration (Kc) for thiamine diphosphate is 2000fold higher than that of wild-type cALS
E49A
-
the mutation causes a 190fold reduction in affinity for thiamine diphosphate
E49D
-
site-directed mutagenesis, the mutant exhibits normal substrate kinetics, with the Km for pyruvate equal to that of wild-type cALS
E49D
-
the mutation causes a 150fold reduction in affinity for thiamine diphosphate
E49Q
-
site-directed mutagenesis, the mutant shows decreased activities and weakened thiamine diphosphate binding, the Kc for ThDP that is 3600fold higher than that of wild-type cALS
E49Q
-
the mutant causes a 170fold reduction in affinity for thiamine diphosphate shows 7% of wild type activity
H111F
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
H111F
the mutant displays 26fold increase in Km value compared to the wild type enzyme
H111R
site-directed mutagenesis, the mutant enzyme exhibits increasedspecific activity and kcat compared to the wild-type enzyme
H111R
the mutant displays 17fold increase in Km value compared to the wild type enzyme
Q112E
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
Q112E
the mutant exhibits significantly lower specific activity with 70fold higher Ks for thiamine diphosphate compared to the wild type enzyme
Q112N
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
Q112N
the mutant exhibits significantly lower specific activity with 15fold higher Ks for thiamine diphosphate compared to the wild type enzyme
Q112V
site-directed mutagenesis, the mutant enzyme exhibits about 50fold lower specific activity with significant reduction in kcat compared to the wild-type enzyme
Q112V
the mutant exhibits significantly lower specific activity with 10fold higher Ks for thiamine diphosphate compared to the wild type enzyme
Q411E
site-directed mutagenesis, the mutant enzyme exhibits increased specific activity and kcat compared to the wild-type enzyme
Q411E
the mutant shows a 10fold rise in Km and a 20fold increase in Ks for thiamine diphosphate compared to the wild type enzyme
Q411N
site-directed mutagenesis, the mutant enzyme has a 3fold increased Km compared to the wild-type enzyme
Q411N
the mutant exhibits increased specific activity and kcat compared to the wild type enzyme
E47A
-
8% activity compared to wild-type
E47A
-
about 5% of wild-type activity
E47Q
-
10% activity compared to wild-type
E47Q
-
about 5% of wild-type activity
V375A
-
mutation in isozyme AHAS II, allows 2-oxo-butanoate to be a good first substrate and the mutant enzyme can synthesize 2-propionyl-2-hydroxybutanoate
V375A
-
slightly reduced kcat value with a moderate increase of the apparent KM of pyruvate. The specificity for 2-ketobutyrate as acceptor is not altered
W464L
-
decrease in activity, increase in Km-value
W464L
-
the mutant of isozyme AHAS II has lost the preference for 2-ketobutyrate as second substrate
W464L
-
naturally occuring mutation
E85A
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate, , the enzyme shows reduced activity compared to the wild-type enzyme
E85A
the mutation leads to severe drop in catalytic activity (0.08% of wild type activity) with reduced affinity toward thiamine diphosphate
E85A
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
E85D
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate
E85D
the mutation leads to severe drop in catalytic activity (2.23% of wild type activity) with reduced affinity toward thiamine diphosphate
E85Q
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate
E85Q
the mutation leads to severe drop in catalytic activity (1.2% of wild type activity) with reduced affinity toward thiamine diphosphate
H84A
site-directed mutagenesis, the mutation leads to the loss of many hydrogen bonds among residues His84, Glu85, and Gln86 in wild-type enzyme
H84A
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
H84T
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
H84T
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
P126E
inactive
P126E
site-directed mutagenesis, inactive mutant
P126T
site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward thiamine diphosphate as cofactor
P126T
the mutant exhibits significantly lower activity than the wild type enzyme
P126V
site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward pyruvate as substrate
P126V
the mutant exhibits significantly lower activity than the wild type enzyme
Q86A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
Q86A
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
Q86W
site-directed mutagenesis, inactive mutant
Q86W
the mutation completely abolishes the enzyme's activity
E85Q
-
site-directed mutagenesis, the mutation leads to severe drop in catalyticactivity with reduced affinity toward thiamine diphosphate
-
E85Q
-
the mutation leads to severe drop in catalytic activity (1.2% of wild type activity) with reduced affinity toward thiamine diphosphate
-
H84A
-
site-directed mutagenesis, the mutation leads to the loss of many hydrogen bonds among residues His84, Glu85, and Gln86 in wild-type enzyme
-
H84A
-
the mutation leads to severe drop in catalytic activity with reduced affinity toward thiamine diphosphate
-
P126E
-
site-directed mutagenesis, inactive mutant
-
P126T
-
site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward thiamine diphosphate as cofactor
-
P126T
-
the mutant exhibits significantly lower activity than the wild type enzyme
-
P126V
-
site-directed mutagenesis, the mutant exhibits significantly lower activity than wild-type enzyme and a significantly decreased preference toward pyruvate as substrate
-
P126V
-
the mutant exhibits significantly lower activity than the wild type enzyme
-
P197E
site-directed mutagenesis, the mutation confers broad-spectrum resistance across ALS inhibitors. A subpopulation (WRR04) is generated and is individually homozygous for the Pro197Glu substitution. The WRR04 population exhibits broad-spectrum resistance to tribenuron (318fold), pyrithiobac sodium (over 197fold), pyroxsulam (81fold), florasulam (over 36fold) and imazethapyr (11fold). The ALS from WRR04 shows high resistance to all the tested ALS inhibitors
P197E
the mutation leads to high resistance to inhibitors tribenuron, pyrithiobac sodium, pyroxsulam (TP, 81-fold), florasulam, and imazethapyr
D374A
-
substrate inhibition at high concentrations, strong resistance to Londax and Cadre, 10fold increase in activation efficiency for thiamine diphosphate
D374A
-
naturally occuring mutation
D375A
-
about 10fold increase in Km-value, strong resistance to Londax
D375A
-
naturally occuring mutation
D375E
-
about 3fold reduction in Km-value, strong resistance to Londax, about 3fold increase in activation efficiency of FAD
D375E
-
naturally occuring mutation
H351Q
-
60fold increase in Km-value, strong resistance to Londax and Cadre, difference in secondary structure compared to wild-type
H351Q
-
naturally occuring mutation
K255F
-
strong resistance to Londax, Cadre and N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
K255F
-
naturally occuring mutation
K255Q
-
strong resistance to Londax, Cadre and N-(4,6-dimethylpyrimidin-2-yl)-5-methyl-6,7,8,8a-tetrahydro-5aH-cyclopenta[e][1,2,4]triazolo[1,5-a]pyrimidine-2-sulfonamide
K255Q
-
naturally occuring mutation
S627I
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
S627I
-
the mutation contributes to herbicide resistance
W548L
the naturally occuring mutation reduces the enzyme's sensitivity to herbicides
W548L
-
the mutation contributes to herbicide resistance
W548L/S627I
a naturally occuring mutation, the recombinant enzyme shows resistance to multiple herbicides including pyrimidinylcarboxylate, sulfonylurea and imidazolinone herbicides, and shows stronger resistance to pyrimidinylcarboxylate herbicides than to other herbicides. Bispyribac-sodium, a pyrimidinylcarboxylate herbicide, has almost no effect on the enzyme at up to 100m M, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type. The resistance level of the double mutant W548L/S627I BS is stronger than the additive effect predicted from the degree of resistance of each single amino acid mutated ALS, phenotype, overview
W548L/S627I
mutant confers resistance to multiple herbicides including pyrimidinylcarboxylate, sulfonylurea and imidazolinone herbicides, and shows stronger resistance to pyrimidinylcarboxylate herbicides than to other herbicides. Bispyribac-sodium has almost no effect on the enzyme even at 100 mM, which is an approximately 10000fold higher concentration than the concentration required for 50% inhibition of the wild-type. The resistance level of W548L/S627I is stronger than the additive effect predicted from the degree of resistance of each single amino acid mutated. Transformed rice cells carrying this gene and a regenerated rice plant express resistance to bispyribac-sodium
W548L/S627I
-
use of two-point mutated gene of acetolactate synthase from herbicide-resistant rice callus as a selectable marker gene in production of transgenic soybeans. T1 soybeans grown from one regenerated plant after selection of the acetolactate synthase targeting pyrimidinyl-carboxy herbicide bispyribacsodium exhibit herbicide resistance, and the introduction and expression of the gene is confirmed by genetic analysis. The selective culturing is applicable to the production of transgenic soybeans
A205F
the A205F substitution in acetolactate synthase, confirmed in a population of allotetraploid annual bluegrass, confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
A205F
the A205F substitution in acetolactate synthase, confirmed in a population of allotetraploid annual bluegrass, confers resistance to imidazolinone, sulfonylurea, triazolopyrimidines, sulfonylaminocarbonyl triazolinones, and pyrimidinyl(thio)benzoate herbicides
A205F
the mutation confers high resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
W574L
the mutation confers resistance to imidazolinones, sulfonylureas, triazolopyrimidines, sulfonylamino-carbonyl-triazolinones, and pyrimidinyl (thio) benzoate herbicides
W574L
-
the mutation causes herbicide resistance. The mutant enzyme is over 9000fold more resistant towards metsulfuron-methyl and imazethapyr than the wild type enzyme
P197S
naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron
P197S
the mutant shows increased resistance against imazosulfuron
P197T
naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron
P197T
the mutant shows increased resistance against imazosulfuron
W574L
naturally occuring mutation leading to resistance against the sulfonylurea herbicide imazosulfuron
W574L
the mutant shows increased resistance against imazosulfuron
DeltaQ217
mutation in subunit ilvB, mutant enzyme is activated by valine and resisitant to 3-chlorobutanoate and norleucine
DeltaQ217
mutation in the beta-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit
E139A
mutation in a conservative loop near the active center, mutant enzyme is activated by valine and resistant to 2-oxobutanoate
E139A
mutation in the alpha-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit
L18F
no enzymic activity after in vitro reconstitution with large subunit
L18F
mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation does not influence the interaction of the subunits
V17D
no enzymic activity after in vitro reconstitution with large subunit
V17D
mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits
H474R
site-directed mutagenesis
H474R
the mutant shows reduced activity compared to the wild type enzyme
H474R
site-directed mutagenesis, the reaction specificity of acetolactate synthase from Thermus thermophilus is redirected to catalyze acetaldehyde formation to develop a thermophilic pyruvate decarboxylase. The mutation likely generates two new hydrogen bonds near the thiamine diphosphate-binding site. These hydrogen bonds might result in the better accessibility of H+ to the substrate-cofactor-enzyme intermediate and a shift in the reaction specificity of the enzyme
K139R
site-directed mutagenesis
K139R
the mutant shows slightly reduced activity compared to the wild type enzyme
V172A
site-directed mutagenesis
V172A
the mutant shows reduced activity compared to the wild type enzyme
Y35N
site-directed mutagenesis
Y35N
the mutant shows reduced activity compared to the wild type enzyme
Y35N/K139R/V172A/H474R
the mutant shows strongly reduced activity compared to the wild type enzyme
Y35N/K139R/V172A/H474R
shows 3.1fold higher acetaldehyde-forming activity than the wild-type
K139R
-
site-directed mutagenesis
-
K139R
-
the mutant shows slightly reduced activity compared to the wild type enzyme
-
additional information
-
identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
-
substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
additional information
-
substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
-
additional information
structure-guided mutagenesis strategy to generate enzyme AlsS variants
additional information
-
structure-guided mutagenesis strategy to generate enzyme AlsS variants
additional information
-
structure-guided mutagenesis strategy to generate enzyme AlsS variants
-
additional information
-
identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
-
mutations of the residues M8 and M13 of the small, regulatory subunit encoded by gene ilvN result in reduced sensitivity of the mutant enzymes to feedback inhibition which leads to increased production of valine as well as of isoleucine and leucine
additional information
-
construction of a mutant with a deleted C-terminal domain in the regulatory subunit IlvN. The constructed enzyme shows altered kinetic properties, i.e., an about twofold-lower Km for the substrate pyruvate and an about fourfold-lower Vmax, a slightly increased Km for the substrate alpha-ketobutyrate with an about twofold-lower Vmax, and insensitivity against the inhibitors L-valine, L-isoleucine, and L-leucine. Introduction of the mutant into the L-lysine producers Corynebacterium glutamicum DM1729 and DM1933 increases L-lysine formation by 43% and 36%, respectively. Complete inactivation of the AHAS in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit of AHAS, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to further-improved L-lysine production. In batch fermentations, the mutant produces about 85% more L-lysine and shows an 85%-higher substrate-specific product yield
additional information
-
the 138th (alanine) and 404th (valine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme
additional information
-
the 138th (valine) and 404th (alanine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme. The 138th valine of subunit IlvB is beneficial for the L-valine biosynthesis
additional information
-
the 138th (alanine) and 404th (valine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme
-
additional information
-
the 138th (valine) and 404th (alanine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme. The 138th valine of subunit IlvB is beneficial for the L-valine biosynthesis
-
additional information
-
the 138th (alanine) and 404th (valine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme
-
additional information
-
the 138th (valine) and 404th (alanine) residues in the subunit IlvB play important roles in the substrate preference of the condensation reaction catalyzed by the enzyme. The 138th valine of subunit IlvB is beneficial for the L-valine biosynthesis
-
additional information
-
the aspartate substitution significantly affects the activation of thiamine diphosphate. The Kc for thiamine diphosphate is determined to be 280fold higher than that of wild-type cALS
additional information
-
isozyme AHAS II mutants of residues Phe109, Met250, Arg276 and Trp464 are nearly inactive in (S)-2-acetolactate formation, but show increased activity with pyruvate and benzaldehyde compared to the wild-type isozyme
additional information
-
the truncated mutant DELTA80 is resistant to inhibition by valine
additional information
-
identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
-
identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
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mutants with overexpression of 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase, and acetoin reductase, either individually or in combination, are constructed to improve 2,3-butanediol production in Klebsiella pneumoniae. The strain (KG-rs) that overexpresses both 2-acetolactate synthase and acetoin reductase shows an improved 2,3-butanediol yield. When cultured in the media with five different carbon sources (glucose, galactose, fructose, sucrose, and lactose), the mutant exhibits higher 2,3-butanediol productivity and production than the parental strain in all the tested carbon sources except for lactose. The 2,3-butanediol production of strain KG-rs in a batch fermentation with glucose as the carbon source is 12% higher than that of the parental strain, overview
additional information
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mutants with overexpression of 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase, and acetoin reductase, either individually or in combination, are constructed to improve 2,3-butanediol production in Klebsiella pneumoniae. The strain (KG-rs) that overexpresses both 2-acetolactate synthase and acetoin reductase shows an improved 2,3-butanediol yield. When cultured in the media with five different carbon sources (glucose, galactose, fructose, sucrose, and lactose), the mutant exhibits higher 2,3-butanediol productivity and production than the parental strain in all the tested carbon sources except for lactose. The 2,3-butanediol production of strain KG-rs in a batch fermentation with glucose as the carbon source is 12% higher than that of the parental strain, overview
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additional information
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mutants with overexpression of 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase, and acetoin reductase, either individually or in combination, are constructed to improve 2,3-butanediol production in Klebsiella pneumoniae. The strain (KG-rs) that overexpresses both 2-acetolactate synthase and acetoin reductase shows an improved 2,3-butanediol yield. When cultured in the media with five different carbon sources (glucose, galactose, fructose, sucrose, and lactose), the mutant exhibits higher 2,3-butanediol productivity and production than the parental strain in all the tested carbon sources except for lactose. The 2,3-butanediol production of strain KG-rs in a batch fermentation with glucose as the carbon source is 12% higher than that of the parental strain, overview
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additional information
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identification of naturally occuring mutations leading to herbicide resistance of the plants, e.g. chlorsulfuron-resistant plants, overview. ALS-inhibiting herbicides occur in Lactuca serriola within a relatively small geographical area
additional information
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identification and phenotypes of herbicide-resistant mutant enzymes, overview
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several mutations, including deletion mutations W548deletion, P171deletion and S627deletion, reduce the enzyme's sensitivity to herbicides, overview
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among 28 populations resistant to herbiced tribenuron, nine individuals have only the mutant ALS gene and are homozygous, 18 individuals have both the wild type and the mutant ALS gene and are heterozygous, whereas one individual is heterozygous but with two different mutant ALS alleles
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cloning of a herbicide-resistant acetohydroxyacid synthase gene from Pseudomonas sp. Lm10. Sequence analysis shows that the regulatory subunit of the resisitant enzyme is identical to that of Pseudomonas putida KT2440, whereas six mutations are found in the catalytic subunit, i.e. resistant AHAS/sensitive AHAS: H134N, A135P, S136T, I210V, F264Y, and S486W
additional information
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cloning of a herbicide-resistant acetohydroxyacid synthase gene from Pseudomonas sp. Lm10. Sequence analysis shows that the regulatory subunit of the resisitant enzyme is identical to that of Pseudomonas putida KT2440, whereas six mutations are found in the catalytic subunit, i.e. resistant AHAS/sensitive AHAS: H134N, A135P, S136T, I210V, F264Y, and S486W
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additional information
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generation of the deletion mutants DELTAMoilv2 and DELTAMoilv6. Phenotypic analysis shows that both mutants are auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity
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generation of the deletion mutants DELTAMoilv2 and DELTAMoilv6. Phenotypic analysis shows that both mutants are auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity
additional information
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generation of the deletion mutants DELTAMoilv2 and DELTAMoilv6. Phenotypic analysis shows that both mutants are auxotrophic for leucine, isoleucine and valine, and are defective in conidial morphogenesis, appressorial penetration and pathogenicity
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additional information
engineering of a strain of Pyrococcus furiosus to contain an additional pathway for ethanol production. Enzyme ALS deletion abolishes acetoin formation and improves ethanol production in the alcohol dehydrogenase ADHA strain. High level expression of enzyme ALS uncouples the temperature-dependence of acetoin formation
additional information
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engineering of a strain of Pyrococcus furiosus to contain an additional pathway for ethanol production. Enzyme ALS deletion abolishes acetoin formation and improves ethanol production in the alcohol dehydrogenase ADHA strain. High level expression of enzyme ALS uncouples the temperature-dependence of acetoin formation
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identification and phenotypes of herbicide-resistant mutant enzymes, overview
additional information
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expression of an Ilv2 variant that lacks the N-terminal mitochondrial targeting sequence leads to highly elevated diacetyl levels comparable to a petite strain. Expression of a mutant allele of the gamma-subunit of the F1-ATPase, ATP3-5, could be an attractive way to reduce diacetyl formation by petite strains
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shortening of the regulatory subunit to 107 residues reduces the interaction with the catalytic subunit essentially
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shortening of the regulatory subunit to 107 residues reduces the interaction with the catalytic subunit essentially
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genotyping by random mutagenesis, error-prone PCR and mutant library screening leading to the identification of a quadruple mutant with 3.1fold higher acetaldehyde-forming activity than the wild-type, mutant reaction-specificity profiles
additional information
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genotyping by random mutagenesis, error-prone PCR and mutant library screening leading to the identification of a quadruple mutant with 3.1fold higher acetaldehyde-forming activity than the wild-type, mutant reaction-specificity profiles
additional information
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genotyping by random mutagenesis, error-prone PCR and mutant library screening leading to the identification of a quadruple mutant with 3.1fold higher acetaldehyde-forming activity than the wild-type, mutant reaction-specificity profiles
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