2.2.1.6: acetolactate synthase
This is an abbreviated version!
For detailed information about acetolactate synthase, go to the full flat file.
Word Map on EC 2.2.1.6
-
2.2.1.6
-
herbicide
-
weed
-
sulfonylurea
-
als-inhibiting
-
branched-chain
-
imidazolinone
-
biotype
-
cross-resistance
-
herbicide-resistant
-
imazethapyr
-
chlorsulfuron
-
triazolopyrimidine
-
4.1.3.18
-
als-inhibitors
-
glyphosate
-
target-site
-
amaranthus
-
imazamox
-
acetoin
-
sulfometuron
-
2,3-butanediol
-
echinochloa
-
protoporphyrinogen
-
broadleaf
-
2-ketobutyrate
-
non-target-site
-
whole-plant
-
nicosulfuron
-
accase
-
hybridus
-
rigidum
-
waterhemp
-
mesotrione
-
postemergence
-
crus-galli
-
safener
-
5-enolpyruvylshikimate-3-phosphate
-
ilvced
-
alpha-ketobutyrate
-
brewing
-
rudis
-
dicamba
-
synthesis
-
agriculture
-
molecular biology
-
glufosinate
-
thdp-dependent
-
palmeri
-
tuberculatus
-
analysis
-
alopecurus
-
isomeroreductase
-
pharmacology
-
herbicide-binding
-
drug development
-
glyphosate-resistant
-
kochia
-
biotechnology
- 2.2.1.6
-
herbicide
-
weed
- sulfonylurea
-
als-inhibiting
-
branched-chain
- imidazolinone
-
biotype
-
cross-resistance
-
herbicide-resistant
- imazethapyr
- chlorsulfuron
- triazolopyrimidine
-
4.1.3.18
-
als-inhibitors
- glyphosate
-
target-site
- amaranthus
- imazamox
- acetoin
- sulfometuron
- 2,3-butanediol
- echinochloa
- protoporphyrinogen
-
broadleaf
- 2-ketobutyrate
-
non-target-site
-
whole-plant
- nicosulfuron
- accase
- hybridus
- rigidum
-
waterhemp
- mesotrione
-
postemergence
- crus-galli
-
safener
- 5-enolpyruvylshikimate-3-phosphate
-
ilvced
- alpha-ketobutyrate
- brewing
- rudis
- dicamba
- synthesis
- agriculture
- molecular biology
- glufosinate
-
thdp-dependent
- palmeri
- tuberculatus
- analysis
-
alopecurus
-
isomeroreductase
- pharmacology
-
herbicide-binding
- drug development
-
glyphosate-resistant
- kochia
- biotechnology
Reaction
2 pyruvate
=
Synonyms
aceto-hydroxy acid synthase, acetohydroxy acid synthase, acetohydroxy acid synthase I, acetohydroxy acid synthetase, acetohydroxyacid synthase, acetolactate pyruvate-lyase (carboxylating), acetolactate synthase, acetolactate synthetase, acetolactate-synthase, acetolactic synthetase, AHAS, AHAS II, AHAS1, AHAS2, AHAS3, AHASL, AHASS, alpha-acetohydroxy acid synthetase, alpha-acetohydroxyacid synthase, alpha-acetolactate synthase, alpha-acetolactate synthetase, alpha-ALS, ALS, ALS1, ALS1R, ALS2, AlsS, CalS, catabolic acetolactate synthase, EC 4.1.3.18, GST-mALS, GST-wALS, Ilv2, Ilv6, ilvB, ilvB1, ilvB2, ilvG, IlvN, ilvX, Moilv2, Moilv6, More, PF0935, sll1981, synthase, acetolactate, TM_0548, TM_0549, TTHA1213
ECTree
2.2.1.6 acetolactate synthaseAdvanced search results
results (
results (Cofactor
Cofactor on EC 2.2.1.6 - acetolactate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
O2
each subunit contains two molecules of oxygen (O2(I) and O2(II))
FAD
-
partial requirement for isoenzyme III
FAD
-
absolutly required for isoenzyme I and II, no requirement for isoenzyme III
FAD
-
contains bound FAD, 0.88 mol per mol of protomer of 69000 Da
FAD
-
required for the enzyme in anabolic function, but not in catabolic function, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview
FAD
-
the flavin plays a crucial role in the structural integrity, and is reduced in the course of catalysis as a result of an internal redox side reaction
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
-
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
required, presence of FAD in AHAS is an evolutionary relic of the ancestry of its sub-family of ThDP-dependent enzymes, binding structure, overview
FAD
-
the secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface
FAD
-
the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct
FAD
-
the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct
FAD
the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct
FAD
-
the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct, reaction mechanism molecular modeling
FAD
the anabolic enzyme form is dependent on the presence of FAD, structure of the enamine-FAD adduct, reaction mechanism molecular modeling
thiamine diphosphate
-
required as cofactor
thiamine diphosphate
-
Km: 0.0087 mM for isoenzyme I, 0.026 mM for isoenzyme III
thiamine diphosphate
-
dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group
thiamine diphosphate
-
the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
-
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
required, ThDP is anchored in the active site by a divalent metal ion cofactor such as Mg2+
thiamine diphosphate
Ks value 0.042 mM
thiamine diphosphate
-
residue Glu47 is involved in cofactor activation, substrate binding, and product elimination and plays a crucial catalytic role in the carboligation of the acceptor and the hydroxyethyl-thiamine diphosphate enamine intermediate. The Glu47-cofactor proton shuttle acts in concert with Gln110 in the carboligation
thiamine diphosphate
dependent on, located centrally in the active site of cALS with a unique V-conformation at the dimer interface to play a central role of intramolecular protontransfer in the catalytic cycle. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catalbolic enzyme
thiamine diphosphate
dependent on, the cofactor plays a key role in catalysis. The thiamine diphosphate binding pocket contains the highly conserved proline 126 residue, binding pocket structure, overview. Thiamine diphosphate is located centrally in the active site of AHAS with a unique V-conformation at the dimer interface. In the dimeric structure, one subunit is in contact with the diphosphate moiety of thiamine diphosphate, and the other subunit is in contact with the aminopyrimidine moiety
thiamine diphosphate
dependent on, the thiamine function of ThDP interacts with residues of one monomer and the adjacent monomer
thiamine diphosphate
dependent on, TPP binding site of the model structure of enzyme TtALS, overview
thiamine diphosphate
-
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
thiamine diphosphate
-
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
thiamine diphosphate
-
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
thiamine diphosphate
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
thiamine diphosphate
dependent on, upon removal of the cofactor, the activity of the enzyme is completely abolished and again restored by readdition of thiamine diphosphate. ThDP has a central role in the enzyymes catalytic mechanism. In the active site of enzyme, it is located at its centre with a unique V-conformation at the dimer interface. Decarboxylation of pyruvate is carried out by ThDP
thiamine diphosphate
K0.5 value for holoenzyme 0.0055 mM, for the isolated large subunit 0.24 mM
additional information
-
spectral analysis and kinetics of cofactor binding, overview
-
additional information
-
the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer
-
