2.6.1.42: branched-chain-amino-acid transaminase
This is an abbreviated version!
For detailed information about branched-chain-amino-acid transaminase, go to the full flat file.
Word Map on EC 2.6.1.42
-
2.6.1.42
-
bcats
-
isoleucine
-
transamination
-
aminotransferases
-
pyridoxal
-
ketoacids
-
alpha-ketoisocaproate
-
transaminases
-
l-valine
-
isomeroreductase
-
gabapentin
-
acetohydroxy
-
alpha-ketoacids
-
nutrition
-
synthesis
-
acetohydroxyacid
-
medicine
-
drug development
-
analysis
- 2.6.1.42
-
bcats
- isoleucine
-
transamination
- aminotransferases
- pyridoxal
-
ketoacids
- alpha-ketoisocaproate
- transaminases
- l-valine
-
isomeroreductase
- gabapentin
-
acetohydroxy
- alpha-ketoacids
- nutrition
- synthesis
-
acetohydroxyacid
- medicine
- drug development
- analysis
Reaction
Synonyms
(R)-selective omega-aminotransferase, AGT, alpha-KGA, At1g50110, At5g17310, Bat1, Bat1p, BAT2, Bat2p, BCAA, BCAA aminotransferase, BCAA-AT, BCAATase, BcaT, BCAT-1, BCAT1, Bcat2, BCAT4, Bcat6, BCAT7, BCATc, BCATm, branched chain amino acid: 2-oxoglutarate aminotransferase EC 2.6.1, branched chain aminotransferase, branched chain aminotransferase IlvE, branched chain aminotransferase, cytosolic isoform, branched chain aminotransferase, mitochondrial isoform, branched-chain amino acid aminotransferase, branched-chain amino acid aminotransferase 1, branched-chain amino acid aminotransferase 2, branched-chain amino acid aminotransferase 3, branched-chain amino acid aminotransferase 4, branched-chain amino acid aminotransferase 5, branched-chain amino acid aminotransferase 6, branched-chain amino acid transaminase, branched-chain amino acid transaminase 1, branched-chain amino acid transferase, branched-chain amino acid-glutamate transaminase, branched-chain amino-acid aminotransferase, branched-chain amino-acid transaminase, branched-chain aminotransferase, branched-chain aminotransferase 7, branched-chain aminotransferase4, CsBCAT2, CsBCAT3, CsBCAT7, eBCAT, EC 2.6.1.6, glutamate-branched-chain amino acid transaminase, hBCAT, hBCATm, Hoch3033, IlvE, IlvE aminotransferase, ilvE1, L-branched chain amino acid aminotransferase, L-leucine-alpha-ketoglutarate transaminase, leucine aminotransferase, leucine transaminase, Mevan_0408, mitochondrial branched chain aminotransferase, More, MtIlvE, PsBCAT, R-omegaAT, R-omegaAT_Bcel, R-omegaAT_Bthu, Rv2210c, SlBCAT1, SlBCAT2, SlBCAT3, SlBCAT4, SlBCAT5, SlBCAT6, SpBCAT1, TA-B, transaminase B, trd_1610, Tter_1720, TUZN1299, VMUT0738, VMUT_0738
ECTree
2.6.1.42 branched-chain-amino-acid transaminaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.6.1.42 - branched-chain-amino-acid transaminase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-alpha-ethylbenzylamine + 3-methyl-2-oxovalerate
alpha-ethylbenzaldehyde + L-isoleucine
reaction of (R)-amine:pyruvate transaminase, EC 2.6.1.B21
-
-
r
(R)-alpha-methylbenzylamine + 3-methyl-2-oxovalerate
acetophenone + L-isoleucine
reaction of (R)-amine:pyruvate transaminase, EC 2.6.1.B21
-
-
r
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
2-oxo-3-methylvalerate + glyoxalate
L-isoleucine + glycine
-
-
-
r
2-oxo-6-hydroxyhexanoic acid + L-glutamate
L-6-hydroxynorleucine + 2-oxoglutarate
-
-
-
-
?
4,4-dimethyl-2-oxopentanoate + L-glutamate
L-neopentylglycine + 2-oxoglutarate
-
-
-
?
4,4-dimethyl-2-oxovalerate + L-glutamate
L-neopentylglycine + 2-oxoglutarate
-
-
-
r
4-methylthio-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
-
-
r
DL-2-aminoadipate + 2-oxoglutarate
3-oxohexanedioic acid + L-glutamate
-
heart enzyme
-
-
r
DL-2-aminoheptanoate + 2-oxoglutarate
2-oxoheptanoate + L-glutamate
-
-
-
r
DL-2-aminooctanoate + 2-oxobutanoate
2-oxooctanoate + L-2-aminobutanoate
-
-
-
r
DL-2-aminopimelate + 2-oxoglutarate
2-oxoheptanedioate + L-glutamate
-
heart enzyme
-
-
r
DL-allo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
heart enzyme
-
-
r
DL-lysine + 4-methyl-2-oxovalerate
2-oxo-6-aminohexanoate + L-leucine
-
-
-
r
DL-tryptophan + pyruvate
2-oxo-3-indolylpropanoate + L-alanine
-
-
-
r
L-2-aminobutanoate + 4-methylthio-2-oxo-butanoate
2-oxobutanoate + L-methionine
-
-
-
-
r
L-2-aminobutanoate + phenylpyruvate
2-oxobutanoate + L-phenylalanine
-
-
-
r
L-2-aminobutyrate + 4-methyl-2-oxopentanoate
2-oxobutanoate + L-leucine
-
-
-
-
r
L-allo-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
-
r
L-allo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-allo-isoleucine + 2-oxohexanoate
3-methyl-2-oxopentanoate + 2-aminohexanoate
-
-
-
-
r
L-allo-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-allo-isoleucine + 2-oxoisopentanoate
3-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-allo-isoleucine + 2-oxooctanoate
3-methyl-2-oxopentanoate + 2-aminooctanoate
-
-
-
-
r
L-arginine + 2-oxoglutarate
2-oxo-5-guanidinopentanoate + L-glutamate
-
-
-
-
r
L-asparagine + 2-oxoglutarate
2,4-dioxo-4-aminobutanoate + L-glutamate
-
-
-
-
r
L-cysteine + 4-methyl-2-oxovalerate
2-oxo-3-thiobutyrate + L-leucine
-
-
-
r
L-glutamate + (R)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
L-glutamate + (S)-3-methyl-2-oxopentanoate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
L-glutamate + 2-oxo-3-methylpentanoate
2-oxoglutarate + L-isoleucine
-
-
-
-
r
L-glutamate + 3-methyl-2-oxopentanoate
2-oxoglutarate + L-isoleucine
-
-
-
r
L-glutamine + 2-oxobutyrate
2,5-dioxo-5-aminopentanoate + 2-aminobutyrate
-
-
-
r
L-glutamine + 2-oxoglutarate
2,5-dioxo-5-aminopentanoate + L-glutamate
-
-
-
-
r
L-homomethionine + 2-oxoglutarate
5-methylthio-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-isoleucine + 2-oxobutanoate
3-methyl-2-oxopentanoate + 2-aminobutanoate
-
-
-
-
r
L-isoleucine + 2-oxoisocaproate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-isoleucine + 3-methyl-2-oxobutanoate
3-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-isoleucine + 3-methylthio-2-oxobutanoate
3-methyl-2-oxopentanoate + 2-amino-3-methylthiobutanoate
-
-
-
-
r
L-isoleucine + 3-phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
-
-
r
L-isoleucine + 4-methylthio-2-oxobutyrate
3-methyl-2-oxopentanoate + L-methionine
-
-
-
r
L-isoleucine + oxaloacetate
3-methyl-2-oxopentanoate + L-aspartate
-
brain enzyme
-
-
r
L-leucine + 2-oxo-3-methiobutyrate
2-oxoisohexanoate + L-methionine
-
-
-
-
r
L-leucine + 2-oxo-pentanoate
2-oxoisohexanoate + 2-aminopentanoate
-
-
-
-
r
L-leucine + 2-oxobutyrate
4-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
r
L-leucine + 2-oxohexanoic acid
4-methyl-2-oxopentanoate + 2-aminohexanoic acid
-
214% of the activity with 2-oxoglutarate
-
-
?
L-leucine + 2-oxoisovaleric acid
4-methyl-2-oxopentanoate + 2-aminoisovaleric acid
-
135% of the activity with 2-oxoglutarate
-
-
?
L-leucine + 3-methyl-2-oxopentanoate
2-oxo-4-methylpentanoate + L-isoleucine
-
-
-
-
r
L-leucine + prephenate
2-oxoisohexanoate + 1-(2-amino-2-carboxyethyl)-4-hydroxycyclohexa-2,5-diene-1-carboxylic acid
-
-
-
-
r
L-lysine + 2-oxoglutarate
2-oxo-6-aminohexanoate + L-glutamate
-
-
-
-
r
L-lysine + 4-methyl-2-oxovalerate
2-oxo-6-aminohexanoate + L-leucine
-
-
-
r
L-lysine + pyruvate
2-oxo-6-aminohexanoate + L-alanine
-
-
-
r
L-methionine + 2-oxo-isohexanoate
4-methylsulfanyl-2-oxobutanoate + L-leucine
-
-
-
-
r
L-methionine + 2-oxobutanoate
4-methylthio-2-oxobutanoate + L-2-aminobutanoate
-
-
-
-
r
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
-
-
-
-
r
L-norleucine + 2-oxoisocaproate
2-oxohexanoate + L-leucine
-
-
-
r
L-norvaline + 2-oxocaproate
2-oxopentanoate + 2-aminohexanoate
-
-
-
r
L-phenylalanine + 2-oxovalerate
phenylpyruvate + L-norvaline
-
-
-
r
L-serine + 2-oxoglutarate
3-hydroxy-2-oxopropanoate + L-glutamate
-
-
-
-
r
L-threo-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-threonine + 2-oxobutyrate
2-oxo-3-hydroxybutyrate + 2-aminobutyrate
-
-
-
r
L-valine + 2-oxo-3-methylpentanoate
3-methyl-2-oxobutanoate + L-isoleucine
-
-
-
-
r
L-valine + 2-oxobutyrate
3-methyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
r
L-valine + 3-methyl-2-oxopentanoate
3-methyl-2-oxobutanoate + L-isoleucine
-
-
-
-
r
L-valine + 4-methylthio-2-oxo-butanoate
2-oxoisopentanoate + L-methionine
-
-
-
-
?
pyruvate + L-leucine
L-alanine + 4-methyl-2-oxovalerate
-
-
-
r
S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + ?
S-(1,1,2,2-tetrafluoroethyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-(1,2-dichlorovinyl)-L-cysteine + ?
S-(1,2-dichlorovinyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine + ?
S-(2-chloro-1,1,2-trifluoroethyl)-2-oxo-3-thiopropanoate + ?
-
-
-
-
?
S-methyl-L-cysteine + 2-oxoglutarate
3-(methylthio)-2-oxopropanoic acid + L-glutamate
-
heart enzyme
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + 2-oxoglutarate
acetophenone + L-glutamate
-
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-1-phenylethylamine + pyruvate
acetophenone + L-alanine
(R)-PEA
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
Evansella cellulosilytica ATCC 21833
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
Evansella cellulosilytica FERM P-1141
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
Evansella cellulosilytica JCM 9156
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + 2-oxoglutarate
acetophenone + D-glutamate
very low activity, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
Evansella cellulosilytica ATCC 21833
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
Evansella cellulosilytica FERM P-1141
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
Evansella cellulosilytica JCM 9156
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
acetophenone + D-alanine
the enzyme prefers pyruvate as the amino acceptor with (R)-alpha-methylbenzylamine, reaction of (R)-selective omega-aminotransferase, EC 2.6.1.
-
-
r
(R)-alpha-methylbenzylamine + pyruvate
alpha-methylbenzaldehyde + L-alanine
small but significant activity, the (S)-enantiomer is not a substrate
-
-
?
(R)-alpha-methylbenzylamine + pyruvate
alpha-methylbenzaldehyde + L-alanine
small but significant activity, the (S)-enantiomer is not a substrate
-
-
?
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
-
-
-
-
?
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
-
-
-
-
?
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
-
-
-
-
?
2-methylbenzylamine + 4-methyl-2-oxovalerate
acetophenone + L-leucine
-
-
-
r
2-methylbenzylamine + 4-methyl-2-oxovalerate
acetophenone + L-leucine
-
-
-
r
2-oxo-3-indolylpropanoate + L-leucine
L-tryptophan + 4-methyl-2-oxovalerate
-
-
-
r
2-oxo-3-indolylpropanoate + L-leucine
L-tryptophan + 4-methyl-2-oxovalerate
-
-
-
-
r
2-oxo-3-indolylpropanoate + L-leucine
L-tryptophan + 4-methyl-2-oxovalerate
-
-
-
r
2-oxobutyrate + 2-oxoglutarate
2-aminobutyrate + L-glutamate
-
-
-
r
2-oxobutyrate + L-glutamate
2-aminobutyrate + 2-oxoglutarate
-
-
-
-
r
2-oxobutyrate + L-glutamate
2-aminobutyrate + 2-oxoglutarate
-
-
-
r
2-oxobutyrate + L-leucine
2-aminobutyrate + 4-methyl-2-oxovalerate
-
-
-
r
2-oxobutyrate + L-leucine
2-aminobutyrate + 4-methyl-2-oxovalerate
-
-
-
-
r
2-oxobutyrate + L-leucine
2-aminobutyrate + 4-methyl-2-oxovalerate
-
-
-
r
2-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
r
2-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-isoleucine
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
r
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-leucine
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
2-oxoglutarate + L-valine
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
2-oxoglutarate + L-valine
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
2-oxohexanoate + L-glutamate
L-norleucine + 2-oxoglutarate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
2-oxohexanoate + L-glutamate
norleucine + 2-oxoglutarate
high activity
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
r
3-methyl-2-oxobutanoic acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutanoic acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyrate + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyrate + L-glutamate
L-valine + 2-oxoglutarate
-
the transamination of ketoisovalerate (KIV) to valine is carried out mainly by the transaminase B enzyme, with the transaminase C enzyme playing a minor role
-
-
?
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
?
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
high activity
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
high activity
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
r
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methyl-2-oxovalerate
-
-
-
r
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methyl-2-oxovalerate
-
-
-
-
r
3-methyl-2-oxopentanoate + L-leucine
L-isoleucine + 4-methyl-2-oxovalerate
-
-
-
r
3-methyl-2-oxopentanoic acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxopentanoic acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxopentanoate + L-alanine
L-leucine + pyruvate
-
-
-
r
4-methyl-2-oxopentanoate + L-alanine
L-leucine + pyruvate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
?
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
r
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
-
-
-
r
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
-
-
-
-
r
4-methyl-2-oxopentanoate + L-leucine
L-leucine + 4-methyl-2-oxovalerate
-
-
-
r
4-methyl-2-oxopentanoic acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxopentanoic acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
-
-
-
-
?
4-methylsulfanyl-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
-
-
-
r
4-methylsulfanyl-2-oxobutanoate + L-glutamate
L-methionine + 2-oxoglutarate
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
r
beta-phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
r
glycine + 2-oxoglutarate
glyoxylate + L-glutamate
-
0.4% of the activity with L-isoleucine
-
?
glycine + 2-oxoglutarate
L-glutamic acid + glyoxylate
-
-
-
?
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
-
-
-
-
r
L-2-aminobutyrate + 2-oxoglutarate
2-oxobutanoate + L-glutamate
-
heart enzyme
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
-
-
r
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
no substrate: D-alanine
-
-
?
L-alanine + 4-methyl-2-oxopentanoate
pyruvate + L-leucine
no substrate: D-alanine
-
-
?
L-alanine + 4-methyl-2-oxovalerate
pyruvate + L-leucine
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
1.7% of the activity with L-isoleucine
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
1.7% of the activity with L-isoleucine
-
?
L-cysteine + 2-oxoglutarate
2-oxo-3-thiobutyrate + L-glutamate
-
-
-
r
L-cysteine + 2-oxoglutarate
2-oxo-3-thiobutyrate + L-glutamate
-
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
r
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
mitochondrial enzyme
-
-
r
L-glutamate + 4-methyl-2-oxopentanoate
2-oxoglutarate + L-leucine
-
-
-
r
L-glutamate + 4-methylthio-2-oxo-butanoate
2-oxoglutarate + L-methionine
-
-
-
-
?
L-glutamate + 4-methylthio-2-oxo-butanoate
2-oxoglutarate + L-methionine
-
-
-
-
?
L-histidine + 2-oxoglutarate
2-oxo-3-imidazolpropanoate + L-glutamate
-
-
-
-
r
L-histidine + 2-oxoglutarate
2-oxo-3-imidazolpropanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
-
-
-
r
L-isoleucine + 2-oxo-isopentanoate
2-oxoisohexanoate + L-valine
-
-
-
-
r
L-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
r
L-isoleucine + 2-oxobutyrate
3-methyl-2-oxopentanoate + 2-aminobutyrate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?, r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?, r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
mitochondrial enzyme
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
lower reactivity than other origins
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of L-isoleucine
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxopentanoate
-
-
-
-
?
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 2-oxoisohexanoate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 4-methyl-2-oxovalerate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-isoleucine + 4-methyl-2-oxovalerate
3-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-isoleucine + 4-methylthio-2-oxo-butanoate
3-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-isoleucine + 4-methylthio-2-oxo-butanoate
3-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
?
L-isoleucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
?
L-leucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-leucine + 2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
r
L-leucine + 2-oxo-isohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
r
L-leucine + 2-oxo-isohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 2-oxoglutarate
2-oxoisohexanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step of the synthesis or initial step of the degradation of branched chain amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of branched-chain amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
Escherichia coli W3110 / ATCC 27325
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
Evansella cellulosilytica ATCC 21833
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
Evansella cellulosilytica FERM P-1141
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
Evansella cellulosilytica JCM 9156
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
70.1% of the activity with L-isoleucine
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
70.1% of the activity with L-isoleucine
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
82% of the activity with L-isoleucine
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of the branched-chain amino acids L-valine, L-isoleucine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
last step in the biosynthesis of the branched-chain amino acids L-isoleucine, L-valine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of the branched-chain amino acids L-valine, L-isoleucine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of the branched-chain amino acids L-valine, L-isoleucine and L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
mitochondrial isoenzyme functions in the biosynthesis of L-isoleucine, L-leucine and L-valine, cytoplasmic isoenzyme functions in amino acid catabolism
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
high activity
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
highly preferred substrates
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
key enzyme on the biosynthetic pathway of hydrophobic amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
first step in the metabolism of branched-chain amino acids
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
sole transaminase in fetal rat liver
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
involved in production of fusel alcohols during fermentation
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
biosynthesis of L-leucine
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoic acid + L-glutamate
-
-
-
r
L-leucine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
L-leucine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
L-leucine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
-
-
-
?
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
r
L-leucine + 2-oxoisohexanoate
2-oxoisohexanoate + L-leucine
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
-
r
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
-
?
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
-
-
-
-
r
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-leucine + 4-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-leucine + 4-methyl-2-oxovalerate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
r
L-leucine + 4-methyl-2-oxovalerate
4-methyl-2-oxopentanoate + L-leucine
-
-
-
-
r
L-leucine + 4-methylthio-2-oxo-butanoate
4-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-leucine + 4-methylthio-2-oxo-butanoate
4-methyl-2-oxopentanoate + L-methionine
-
-
-
-
?
L-leucine + DL-2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-leucine + DL-2-oxo-3-methylpentanoate
2-oxoisohexanoate + L-isoleucine
-
-
-
-
r
L-leucine + p-hydroxyphenylpyruvate
2-oxoisohexanoate + L-tyrosine
-
-
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
2-oxo-isohexanoic acid 100%, BCATm relative rate 4%, BCATc 6%
-
-
r
L-leucine + phenylpyruvate
2-oxoisohexanoate + L-phenylalanine
-
-
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
2-oxoglutarate 100%, relative rate 1%
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
2-oxo-isohexanoic acid 100%, BCATm and BCATc, relative rate 6%
-
-
r
L-leucine + pyruvate
2-oxoisohexanoate + L-alanine
-
-
-
r
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
?
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
r
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
?
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
-
-
-
r
L-methionine + 2-oxobutyrate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
-
r
L-methionine + 2-oxobutyrate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
r
L-methionine + 2-oxobutyrate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutyrate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
2.9% of the activity with L-isoleucine
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
2.9% of the activity with L-isoleucine
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
transaminated extremely poorly
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
6% of the activity with L-isoleucine
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
cytoplasmic isoenzyme
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
higher reactivity than other origins
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
transaminated extremely poorly
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylthio-2-oxobutanoate + L-glutamate
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylthio-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-methionine + 4-methyl-2-oxovalerate
4-methylsulfanyl-2-oxobutanoate + L-leucine
-
-
-
r
L-methionine + 4-methyl-2-oxovalerate
4-methylsulfanyl-2-oxobutanoate + L-leucine
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
brain enzyme
-
r
L-norleucine + 4-methyl-2-oxovalerate
2-oxohexanoate + L-leucine
-
-
-
r
L-norleucine + 4-methyl-2-oxovalerate
2-oxohexanoate + L-leucine
-
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-norvaline + 4-methyl-2-oxovalerate
2-oxovalerate + L-leucine
-
-
-
r
L-norvaline + 4-methyl-2-oxovalerate
2-oxovalerate + L-leucine
-
-
-
-
r
L-ornithine + 4-methyl-2-oxovalerate
? + L-leucine
-
-
-
r
L-phenylalanine + 2-oxoglutarate
beta-phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
beta-phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
beta-phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
0.9% of the activity with L-isoleucine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
0.9% of the activity with L-isoleucine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
cytoplasmic isoenzyme
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
-
r
L-phenylalanine + 4-methyl-2-oxovalerate
phenylpyruvate + L-leucine
-
-
-
r
L-phenylalanine + 4-methyl-2-oxovalerate
phenylpyruvate + L-leucine
-
-
-
-
r
L-phenylalanine + 4-methylthio-2-oxo-butanoate
phenylpyruvate + L-methionine
-
-
-
-
?
L-phenylalanine + 4-methylthio-2-oxo-butanoate
phenylpyruvate + L-methionine
-
-
-
-
?
L-threonine + 2-oxoglutarate
2-oxo-3-hydroxybutyrate + L-glutamate
-
-
-
-
r
L-threonine + 2-oxoglutarate
2-oxo-3-hydroxybutyrate + L-glutamate
-
-
-
-
r
L-threonine + 2-oxoglutarate
2-oxo-3-hydroxybutyrate + L-glutamate
-
-
-
r
L-threonine + 4-methyl-2-oxovalerate
2-oxo-3-hydroxybutyrate + L-leucine
-
-
-
r
L-threonine + 4-methyl-2-oxovalerate
2-oxo-3-hydroxybutyrate + L-leucine
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
L-glutamic acid + 3-indole-2-oxopropanoate
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamic acid + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + 2-oxoglutarate
L-glutamic acid + 3-indole-2-oxopropanoate
-
-
-
?
L-tryptophan + pyruvate
2-oxo-3-indolylpropanoate + L-alanine
-
-
-
-
r
L-tryptophan + pyruvate
2-oxo-3-indolylpropanoate + L-alanine
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
-
cytoplasmic isoenzyme
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
reaction of branched-chain amino acid transaminase, EC 2.6.1.42
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
47.9% of the activity with L-isoleucine
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
86% of the activity with L-isoleucine
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
mitochondrial enzyme
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
?
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
biosynthesis of L-valine
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoic acid + L-glutamate
-
-
-
r
L-valine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
L-valine + 2-oxoglutarate
L-glutamate + 3-methyl-2-oxobutanoate
-
-
-
-
?
L-valine + 2-oxoisopentanoate
2-oxoisopentanoate + L-valine
-
-
-
r
L-valine + 4-methyl-2-oxovalerate
3-methyl-2-oxobutanoate + L-leucine
-
-
-
r
L-valine + 4-methyl-2-oxovalerate
3-methyl-2-oxobutanoate + L-leucine
-
-
-
-
r
L-valine + pyruvate
3-methyl-2-oxobutanoate + L-alanine
-
-
-
?
L-valine + pyruvate
3-methyl-2-oxobutanoate + L-alanine
-
-
-
?
norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
-
-
-
r
norvaline + 2-oxoglutarate
2-oxovalerate + L-glutamate
-
-
-
r
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
low activity
-
-
r
trimethylpyruvate + L-glutamate
L-tert-leucine + 2-oxoglutarate
-
-
-
-
?
trimethylpyruvate + L-glutamate
L-tert-leucine + 2-oxoglutarate
-
-
-
-
?
additional information
?
-
-
enzyme may influence methionine levels and play an important role in the metabolism of the nonprotein amino acid alpha-aminobutanoate
-
-
?
additional information
?
-
-
isoform Atbcat-1 is able to initiate degradation of all branched-chain amino acids
-
-
?
additional information
?
-
-
little or no activity is detected with L-isoleucine
-
-
?
additional information
?
-
-
no activity is observed with 6-methylthio-2-oxohexanoate, 3-methyl-2-oxopentanoate, or 3-methyl-2-oxobutyrate
-
-
?
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bthu also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bthu shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bthu also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bthu shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
glycine and D-leucine are no substrates, oxaloacetate, pyruvate and glyoxylate are not amino acceptors
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-norVal = L-norLeu = L-Val > L-Phe > L-Trp > L-Ile > L-Met >> L-Tyr >> L-Ala
-
-
-
additional information
?
-
-
purified enzyme has no measurable L-aspartate-2-oxoglutarate activity
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate (Ile) > 4-methyl-2-oxovalerate (Leu) > 4,4-dimethyl-2-oxovalerate (L-neopentylGly) > 2-oxohexanoate (norLeu) > 3-methyl-2-oxobutanoate (Val) > 2-oxovalerate (norVal) > trimethylpyruvate (L-tert-Leu) > 2-oxobutyrate > pyruvate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Phe > L-Met > L-Tyr > L-Trp
-
-
-
additional information
?
-
Escherichia coli W3110 / ATCC 27325
-
no activity towards L-aspartate
-
-
?
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
Evansella cellulosilytica ATCC 21833
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
Evansella cellulosilytica FERM P-1141
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
Evansella cellulosilytica JCM 9156
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
besides R-omegaAT activity, the enzyme R-omegaAT_Bcel also possesses BCAT (EC 2.6.1.42) activity. The enzyme shows no activity with (S)-alpha-methylbenzylamine. Enzyme R-omegaAT_Bcel shows low R-omegaAT activity. The enzyme does not show any D-alanine aminotransferase (DAT, EC 2.6.1.21) activity
-
-
-
additional information
?
-
-
L-aspartic acid, L-arginine, L-citrulline, L-lysine, L-ornithine, L-alanine, beta-alanine and gamma-aminobutyrate are not amino donors, oxalaceteate and glyoxylate are not amino acceptors, pyruvate is a weak amino acceptor, relative activity 1%
-
-
?
additional information
?
-
-
L-citrulline and L-methionine are poor amino donors
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norLeu > L-norVal > L-Met > L-Phe > L-Asp > L-Trp
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norLeu > L-norVal > L-Met > L-Phe > L-Asp > L-Trp
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
the bifunctional transaminase from myxobacterium Haliangium ochraceum, encoded by gene Hoch3033, is active towards keto analogues of branched-chain amino acids (specific substrates for BCATs, EC 2.6.1.42) and (R)-alpha-methylbenzylamine (specific substrate for (R)-amine:pyruvate transaminases, EC 2.6.1.B21). The enzyme shows no activity with (S)-2-methylbenzylamine, 2-amino-5-methylhexane, 1-methyl-3-phenyl-propylamine, (R)-2-aminohexane, D-alanine, L-beta-leucine, and beta-alanine
-
-
-
additional information
?
-
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met = L-Asp = L-Phe > L-Gly
-
-
-
additional information
?
-
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
no or very weak activity is shown toward L-methionine, L-aspartate, L-phenylalanine, glycine and the D-enantiomers of leucine, isoleucine and valine
-
-
?
additional information
?
-
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
no substrate: L-asparagine, L-histidine, and L-lysine, D-isoleucine, D-leucine, D-valine, as well as both enantiomers of alanine, proline, and serine
-
-
?
additional information
?
-
-
recombinant human BCATm and BCATc have beta-lyase activity towards 3 toxic L-cysteine S-conjugates, S-(1,1,2,2-tetrafluoroethyl)-L-cysteine, S-(1,2-dichlorovinyl)-L-cysteine and S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine and toward 3-chloro-L-alanine, BCATm is also active toward benzothiazolyl-L-cysteine, pyruvate formed from beta-lyase substrates
-
-
?
additional information
?
-
-
transamination activity with oxaloacetate is too low to be evaluated, DL-aminoadipate, glycine, L-phenylalanine, L-tyrosine and L-methionine are no substrates
-
-
?
additional information
?
-
-
novel co-repressor for thyroid hormone nuclear receptors
-
-
?
additional information
?
-
novel co-repressor for thyroid hormone nuclear receptors
-
-
?
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment
-
-
-
additional information
?
-
in addition to this traditional role, BCAT possesses other activities including its role as a cysteine S-conjugate beta-lyase and a thiol disulfide isomerase. Aminotransferase proteins including BCAT have been shown to catalyse beta-lyase reactions with amino acids containing a good leaving group in the beta position. Possible BCAT oxidoreductase activity. BCAT enhances the overall PDI activity and increases the rate of refolding. BCATm may be a chaperone for PDI operating through a thiol disulfide exchange mechanism or independently as an oxidoreductase regulated through the redox environment
-
-
-
additional information
?
-
-
no substrate: phenylalanine, tyrosine, tryptophan, aspartic acid, asparagine
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is 2-oxohexanoate > 2-oxoisovalerate > 2-oxoglutarate > 4-methylthio-2-oxobutyrate > 2-oxobutyrate = 3-methyl-2-oxovalerate = beta-phenylpyruvate >> pyruvate, and for amino acids it is L-Ile > L-Leu = L-Val >> L-Met
-
-
-
additional information
?
-
-
with 2-oxoglutarate as acceptor L-alanine is no substrate, with L-aspartate as amino donor, oxaloacetate is no amino acceptor
-
-
?
additional information
?
-
with 2-oxoglutarate as acceptor L-alanine is no substrate, with L-aspartate as amino donor, oxaloacetate is no amino acceptor
-
-
?
additional information
?
-
-
the substrate preference of 2-oxoacids is 2-oxoglutarate > 4-methyl-2-oxovalerate > 2-oxoisovalerate > 4-methylthio-2-oxobutyrate (Met) > beta-phenylpyruvate (Phe) >> pyruvate, and for amino acids it is L-Ile > L-Leu > L-Val > L-Met > L-Cys > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu = L-Val > L-Ile > L-Tyr > L-Trp > L-Phe
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
-
-
-
additional information
?
-
-
a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
-
-
-
additional information
?
-
MtIlvE is an L-amino acid aminotransferase
-
-
-
additional information
?
-
-
MtIlvE is an L-amino acid aminotransferase
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe
-
-
-
additional information
?
-
a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
-
-
-
additional information
?
-
MtIlvE is an L-amino acid aminotransferase
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is 3-methyl-2-oxovalerate > 4-methyl-2-oxovalerate > 2-oxoisovalerate >> beta-phenylpyruvate > 4-methylthio-2-oxobutyrate, and for amino acids it is L-Ile = L-Leu = L-Val > L-Phe
-
-
-
additional information
?
-
a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates
-
-
-
additional information
?
-
-
purified mitochondrial enzyme is not active with L-phenylalanine
-
-
?
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is specific for 2-oxoglutarate, and for amino acids it is L-Leu > L-Ile > L-Val > L-norVal > L-Met > L-Phe. No activity with L-alanine, L-aspartate, L-glycine, L-serine, L-threonine, L-tryptophan, and L-tyrosine
-
-
-
additional information
?
-
-
evaluation of substrate specificity of PsBCAT. The enzyme is able to catalyze transamination of 19 amino acids, and all 2-oxo acids are capable of serving as amino acceptors. With 2-oxoglutarate as amino acceptor, PsBCAT exhibits maximum activity toward L-allo-isoleucine followed by L-phenylglycine, L-leucine, L-norvaline, L-valine, and L-isoleucine. Despite the considerably lower activity, PsBCAT also shows activities toward L-phenylalanine, L-alanine, and L-tert-leucine, but it is inert to L-tryptophan, L-tyrosine, Lthreonine, L-histidine, and L-lysine. PsBCAT has a broader substrate specificity and prefers to catalyze the transamination of bulked aliphatic amino acids. PsBCAT exhibits no activity with amines in propylamine, aniline, and phenylethylamine, which indicates the carboxyl group is essential for binding in the active site, docking study and analysis of ligand binding structures
-
-
-
additional information
?
-
-
the substrate preference of 2-oxoacids is 2-oxoglutarate > 3-methyl-2-oxobutanoate > 2-oxobutyrate > pyruvate, and for amino acids it is L-Leu >> L-Met > L-Val > L-2-aminobutyrate > L-Thr > L-Phe = L-Ile » L-Ala > L-Arg > L-Trp > L-Asp > L-Ser > L-His > L-Lys
-
-
-
additional information
?
-
-
only little or no activity with L-tryptophan, L-phenylalanine, L-glutamine, L-alanine and L-aspartate, KIC, KIV, DL-2oxo-3-methylpentanoate, 2-oxoglutarate, 2-oxohexanoate, 2-oxopentanoate, 2-oxobutyrate, 2-oxo-3-methiobutyrate, pyruvate or phenylpyruvate are acceptors
-
-
?
additional information
?
-
-
L-leucine is the best substrate for the heart enzyme
-
-
?
additional information
?
-
-
specific for L-leucine, L-isoleucine or L-valine, no other amino acid would serve as an amino donor
-
-
?
additional information
?
-
-
activity less than 3% with glycine, L-alanine, L-lysine, L-phenylalanine, L-tryptophan, D-alloisoleucine, D-valine, D-leucine, L-threonine, L-histidine, L-arginine, L-cysteine, DL-homocyteine, beta-aminoisobutyrate, gamma-aminobutyrate, alpha-aminoisobutyrate, DL-alpha-aminocaprylate, L-serine, DL-homoserine, DL-beta-aminobutyrate, DL-N-hydroxyleucine, DL-N-hydroxyvaline, L-aspartate, L-tyrosine, L-kynurenine, L-ornithine, DL-proline, L-glutamine, L-peniclliamine, DL-methionine sulfone, DL-methionine sulfoxide and DL-beta-hydroxy-leucine
-
-
?
additional information
?
-
-
L-isoleucine is the best substrate for the heart enzyme, L-alanine, aspartic, alpha-amino-butyric acid and gamma-aminobutyric acid, epsilon-aminocaproic acid, L-ornithine, L-methionine and L-phenylalanine are no substrates, pyruvate is not a good acceptor
-
-
?
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
-
the substrate preference of 2-oxoacids is beta-phenylpyruvate > 2-oxobutyrate > 2-oxohexanoate > 2-oxoisovalerate > 4-methyl-2-oxovalerate > 2-oxoglutarate > 2-oxovalerate, and for amino acids it is L-Leu = L-Phe > L-Met > L-norLeu > L-Val > L-norVal > L-Ile > L-2-aminobutyrate >> L-Ala = L-Trp > L-Cys > L-Tyr > L-Thr
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is active with (S)-amine substrates, but also with (R)-amines to a lower extent. No activity with beta-Ala and D-Ala. The enzyme is active towards (R)-PEA and not active towards (S)-PEA. Reaction mechanisms
-
-
-
additional information
?
-
enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed
-
-
-
additional information
?
-
-
enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = 3-methyl-2-oxovalerate = pyruvate, and for amino acids it is L-Met > L-ornithine > L-Thr > L-Val > L-norVal > L-His > L-Ile = L-Leu = L-norLeu > L-Phe > L-Ala > L-Lys
-
-
-
additional information
?
-
enzyme TUZN1299 is highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, L-methionine, L-threonine, L-homoserine, L-glutamine, as well as toward 2-oxobutyrate and keto analogues of BCAAs, whereas L-glutamate and 2-oxoglutarate are not converted in the overall reaction. The enzyme shows the highest specificity to BCAAs and their keto analogues. Glu188 forms a novel binding site for positively charged and polar side-chains of amino acids. Lack of accommodation for 2-oxoglutarate and L-glutamate is due to the unique orientation and chemical properties of residues 102-106 in the loop forming the A-pocket, molecular modelling and molecular mechanism, overview. The productive binding of 2-oxooglutarate and L-glutamate (both featuring negatively charged side-chains) in the active site of PMP-enzyme and PLP-enzyme models, respectively, is not observed
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = 3-methyl-2-oxovalerate = pyruvate, and for amino acids it is L-Met > L-ornithine > L-Thr > L-Val > L-norVal > L-His > L-Ile = L-Leu = L-norLeu > L-Phe > L-Ala > L-Lys
-
-
-
additional information
?
-
enzyme VMUT0738 displays broad and atypical substrate specificity. It shows absence of activity toward acidic substrates, high activity toward basic ones, and low but detectable activity toward the (R)-enantiomer of 2-methylbenzylamine. VMUT0738 shows specificity for typical BCAT substrates, L-branched-chain amino acids (BCAAs) and corresponding keto acids. The same or higher level of activity is observed in the overall reaction with aromatic amino acids, methionine, threonine and 2-aminobuturic acid. But activity with 2-oxoglutarate, which is a typical BCAT amino acceptor, is not detected at a concentration range from 0.5 to 20 mM. VMUT0738 is not active with both the corresponding amino acid Glu and another acidic amino acid (Asp). On the contrary, the specific activity of VMUT0738 with the basic amino acids ornithine, lysine and arginine is high. Enzyme VMUT0738 shows high stereospecificity for L-amino acids, no preference for BCAAs, exhibits unusual substrate specificity toward substrates with a basic side chain, and has no activity toward substrates with an acidic side chain
-
-
-
additional information
?
-
-
enzyme VMUT0738 displays broad and atypical substrate specificity. It shows absence of activity toward acidic substrates, high activity toward basic ones, and low but detectable activity toward the (R)-enantiomer of 2-methylbenzylamine. VMUT0738 shows specificity for typical BCAT substrates, L-branched-chain amino acids (BCAAs) and corresponding keto acids. The same or higher level of activity is observed in the overall reaction with aromatic amino acids, methionine, threonine and 2-aminobuturic acid. But activity with 2-oxoglutarate, which is a typical BCAT amino acceptor, is not detected at a concentration range from 0.5 to 20 mM. VMUT0738 is not active with both the corresponding amino acid Glu and another acidic amino acid (Asp). On the contrary, the specific activity of VMUT0738 with the basic amino acids ornithine, lysine and arginine is high. Enzyme VMUT0738 shows high stereospecificity for L-amino acids, no preference for BCAAs, exhibits unusual substrate specificity toward substrates with a basic side chain, and has no activity toward substrates with an acidic side chain
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = indole-3-pyruvate (L-Trp) > 3-methyl-2-oxovalerate > pyruvate, and for amino acids it is L-Met > L-ornithine > L-Lys > L-Thr > L-Val > L-norVal > L-Ile > L-Leu > L-norLeu > L-Ala > L-Phe > L-Trp
-
-
-
additional information
?
-
the substrate preference of 2-oxoacids is 2-oxobutyrate > 4-methyl-2-oxovalerate = indole-3-pyruvate (L-Trp) > 3-methyl-2-oxovalerate > pyruvate, and for amino acids it is L-Met > L-ornithine > L-Lys > L-Thr > L-Val > L-norVal > L-Ile > L-Leu > L-norLeu > L-Ala > L-Phe > L-Trp
-
-
-
additional information
?
-
enzyme VMUT0738 displays broad and atypical substrate specificity. It shows absence of activity toward acidic substrates, high activity toward basic ones, and low but detectable activity toward the (R)-enantiomer of 2-methylbenzylamine. VMUT0738 shows specificity for typical BCAT substrates, L-branched-chain amino acids (BCAAs) and corresponding keto acids. The same or higher level of activity is observed in the overall reaction with aromatic amino acids, methionine, threonine and 2-aminobuturic acid. But activity with 2-oxoglutarate, which is a typical BCAT amino acceptor, is not detected at a concentration range from 0.5 to 20 mM. VMUT0738 is not active with both the corresponding amino acid Glu and another acidic amino acid (Asp). On the contrary, the specific activity of VMUT0738 with the basic amino acids ornithine, lysine and arginine is high. Enzyme VMUT0738 shows high stereospecificity for L-amino acids, no preference for BCAAs, exhibits unusual substrate specificity toward substrates with a basic side chain, and has no activity toward substrates with an acidic side chain
-
-
-
