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Information on EC 2.2.1.6 - acetolactate synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07342

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EC Tree
IUBMB Comments
This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P07342
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
acetolactate synthase, acetohydroxy acid synthase, alpha-acetolactate synthase, ahas1, ahass, ahas2, ahas ii, acetohydroxy acid synthetase, acetohydroxy acid synthase i, ahas3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetohydroxy acid synthase
-
acetohydroxyacid synthase
-
acetohydroxy acid synthase
-
-
-
-
acetohydroxy acid synthetase
-
-
-
-
acetohydroxyacid synthase
acetolactate pyruvate-lyase (carboxylating)
-
-
-
-
acetolactate synthetase
-
-
-
-
acetolactic synthetase
-
-
-
-
alpha-acetohydroxy acid synthetase
-
-
-
-
alpha-acetohydroxyacid synthase
-
-
-
-
alpha-acetolactate synthase
-
-
-
-
alpha-acetolactate synthetase
-
-
-
-
alpha-ALS
-
-
-
-
GST-mALS
-
-
-
-
GST-wALS
-
-
-
-
synthase, acetolactate
-
-
-
-
additional information
the enzyme belongs to the ThDP-dependent family of enzymes
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
catalytic mechanism and active site structure, covalent intermediates
2 pyruvate = 2-acetolactate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
C-C bond formation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pyruvate:pyruvate acetaldehydetransferase (decarboxylating)
This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-45-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
show the reaction diagram
-
-
-
?
pyruvate + 2-oxobutyrate
2-acetohydroxybutyrate + CO2
show the reaction diagram
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
pyruvate
?
show the reaction diagram
-
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
show the reaction diagram
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
?
pyruvate
(S)-2-acetolactate + CO2
show the reaction diagram
the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
show the reaction diagram
-
-
-
?
pyruvate + 2-oxobutyrate
2-acetohydroxybutyrate + CO2
show the reaction diagram
-
-
-
?
2 pyruvate
2-acetolactate + CO2
show the reaction diagram
2-oxobutyrate + pyruvate
(S)-2-aceto-2-hydroxybutyrate + CO2
show the reaction diagram
-
-
-
-
?
pyruvate
2-acetolactate + CO2
show the reaction diagram
-
the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine
-
-
?
pyruvate
?
show the reaction diagram
-
-
-
-
?
pyruvate + 2-oxobutyrate
2-aceto-2-hydroxybutyrate + CO2
show the reaction diagram
-
irreversible decarboxylation of pyruvate
-
-
ir
pyruvate + pyruvate
2-acetolactate + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
O2
each subunit contains two molecules of oxygen (O2(I) and O2(II))
thiamine diphosphate
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the enzyme requires a divalent metal ion
Ca2+
-
activates
Cd2+
-
activates
MgATP2-
-
activates
Mn2+
-
activates
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dichloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-(1,1-dihydroxyethyl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-(2-bromobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(2-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(3-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(4-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-(difluoromethoxy)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
2-amino-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
2-butoxy-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-butyl-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-(methylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethynylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-hydroxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-iodobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-nitrobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1-methylethoxy)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1H-pyrrol-1-yl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(ethylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfonyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(phenylcarbonyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(propylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(trifluoromethoxy)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-iodobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-nitrobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-phenoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(1-methylethoxy)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(ethylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(methylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(phenylcarbonyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(propylsulfanyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(trifluoromethyl)benzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-ethoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-fluorobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-iodobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methylbenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-nitrobenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-phenoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-propoxybenzoic acid
-
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
-
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
-
5-amino-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-benzyl-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-bromo-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-chloro-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
5-cyano-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
-
8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
chlorimuron ethyl
-
leucine
feedback inhibition
penoxsulam
95% inhibition after 40 min at 0.002 mM
thiencarbazone methyl
94% inhibition after 60 min at 0.002 mM
valine
feedback inhibition, the inhibition by valine is uniquely in fungi reversed by MgATP
bispyribac-sodium
-
-
chlorimuron ethyl
-
-
chlorsulfuron
-
-
isoleucine
-
feedback inhibition
L-valine
-
not inhibitory for catalytic subunit alone, inhibitory for catalytic subunit plus small subunit
leucine
-
feedback inhibition
thiencarbazone methyl
-
-
ubiquinone-1
-
-
valine
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.93
pyruvate
-
-
additional information
additional information
-
kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.62
2-(2-bromobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2.1
2-(2-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2.16
2-(3-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
2.03
2-(4-chlorobenzyl)-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
4.41
2-butyl-8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
7.89
8-[(4,6-dimethoxypyrimidin-2-yl)oxy]-4-methylphthalazin-1(2H)-one
-
0.16
L-valine
-
catalytic subunit plus small subunit, pH 7.0, 30°C
0.003 - 0.177
valine
additional information
additional information
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00603
2,3-dichloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00568
2-(1,1-dihydroxyethyl)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00719
2-(difluoromethoxy)-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00684
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00714
2-acetyl-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.007
2-amino-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00782
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.0074
2-bromo-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.00621
2-butoxy-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00762
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00749
2-chloro-6-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.00633
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.00539
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-3-methylbenzoic acid
Saccharomyces cerevisiae
-
0.00432
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-(methylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00459
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethylbenzoic acid
Saccharomyces cerevisiae
-
0.0047
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-ethynylbenzoic acid
Saccharomyces cerevisiae
-
0.00627
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.0072
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-hydroxybenzoic acid
Saccharomyces cerevisiae
-
0.00505
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-iodobenzoic acid
Saccharomyces cerevisiae
-
0.0046
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methoxybenzoic acid
Saccharomyces cerevisiae
-
0.00503
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-methylbenzoic acid
Saccharomyces cerevisiae
-
0.0039
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-5-nitrobenzoic acid
Saccharomyces cerevisiae
-
0.00573
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1-methylethoxy)benzoic acid
Saccharomyces cerevisiae
-
0.00828
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(1H-pyrrol-1-yl)benzoic acid
Saccharomyces cerevisiae
-
0.00711
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(ethylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00757
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00587
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(methylsulfonyl)benzoic acid
Saccharomyces cerevisiae
-
0.00567
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(phenylcarbonyl)benzoic acid
Saccharomyces cerevisiae
-
0.00629
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(propylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00696
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-(trifluoromethoxy)benzoic acid
Saccharomyces cerevisiae
-
0.00705
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethoxybenzoic acid
Saccharomyces cerevisiae
-
0.00657
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-ethylbenzoic acid
Saccharomyces cerevisiae
-
0.0073
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.00766
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-iodobenzoic acid
Saccharomyces cerevisiae
-
0.00736
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methoxybenzoic acid
Saccharomyces cerevisiae
-
0.00689
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-methylbenzoic acid
Saccharomyces cerevisiae
-
0.00664
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-nitrobenzoic acid
Saccharomyces cerevisiae
-
0.0077
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-phenoxybenzoic acid
Saccharomyces cerevisiae
-
0.00624
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propoxybenzoic acid
Saccharomyces cerevisiae
-
0.00589
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]-6-propylbenzoic acid
Saccharomyces cerevisiae
-
0.00664
2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00488
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(1-methylethoxy)benzoic acid
Saccharomyces cerevisiae
-
0.00667
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(ethylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00768
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(methylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00519
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(phenylcarbonyl)benzoic acid
Saccharomyces cerevisiae
-
0.00572
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(propylsulfanyl)benzoic acid
Saccharomyces cerevisiae
-
0.00602
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-(trifluoromethyl)benzoic acid
Saccharomyces cerevisiae
-
0.0067
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-ethoxybenzoic acid
Saccharomyces cerevisiae
-
0.00767
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-fluorobenzoic acid
Saccharomyces cerevisiae
-
0.00699
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-iodobenzoic acid
Saccharomyces cerevisiae
-
0.00705
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methoxybenzoic acid
Saccharomyces cerevisiae
-
0.00753
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-methylbenzoic acid
Saccharomyces cerevisiae
-
0.00669
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-nitrobenzoic acid
Saccharomyces cerevisiae
-
0.0056
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-phenoxybenzoic acid
Saccharomyces cerevisiae
-
0.00614
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]-6-propoxybenzoic acid
Saccharomyces cerevisiae
-
0.0068
2-[(4,6-dimethoxypyrimidin-2-yl)sulfanyl]benzoic acid
Saccharomyces cerevisiae
-
0.0078
3-[(4,6-dimethoxypyrimidin-2-yl)oxy]biphenyl-2-carboxylic acid
Saccharomyces cerevisiae
-
0.00609
5-amino-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00358
5-benzyl-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.0045
5-bromo-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00535
5-chloro-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
0.00371
5-cyano-2-[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid
Saccharomyces cerevisiae
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49
-
catalytic subunit plus small subunit, pH 7.0, 30°C
6.8
-
catalytic subunit, pH 7.0, 30°C
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
pH 6.0: about 25% of maximal activity, pH 7.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
an N-terminal peptide, which is subsequently removed, is required to direct the protein to mitochondria in fungi
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme catalyzes the first step in biosynthesis of branched amino acids isoleucine, leucine and valine
physiological function
-
deletion of gene ilv2 encoding acetolactate synthase results in loss of viability during isoleucine and valine starvation due to 2-oxobutanoate accumulation. Rapamycin further decreases vialbility of the mutant. Recovery from starvation is influenced by the carbon source present during recovery
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit
75000
-
2 * 75000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit
homodimer
x-ray crystallography
dimer
-
2 * 75000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the N-terminal peptide of the precursor protein is removed
proteolytic modification
-
enzyme contains a N-terminal mitochondrial targeting sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
in complex with penoxsulam, hanging drop vapor diffusion method, using 1.0 M succinic acid, pH 7.0, 0.1 M HEPES, pH 7.0, and 1% (w/v) PEG monomethyl ether 2000
in complex with pyruvate
free enzyme and in complex with inhibitors, hanging drop vapor diffusion method, using 1 M sodium potassium tartrate, 0.1 M CHES and 0.1-0.2 M lithium sulfate
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A117D
naturally occuring mutation
A117E
naturally occuring mutation
A117F
naturally occuring mutation
A117H
naturally occuring mutation
A117I
naturally occuring mutation
A117K
naturally occuring mutation
A117L
naturally occuring mutation
A117M
naturally occuring mutation
A117N
naturally occuring mutation
A117P
naturally occuring mutation
A117Q
naturally occuring mutation
A117R
naturally occuring mutation
A117S
naturally occuring mutation
A117T
naturally occuring mutation
A117V
naturally occuring mutation
A117W
naturally occuring mutation
A117Y
naturally occuring mutation
A200C
naturally occuring mutation
A200D
naturally occuring mutation
A200E
naturally occuring mutation
A200R
naturally occuring mutation
A200T
naturally occuring mutation
A200V
naturally occuring mutation
A200W
naturally occuring mutation
A200Y
naturally occuring mutation
A26V
naturally occuring mutation
D379E
naturally occuring mutation
D379G
naturally occuring mutation
D379N
naturally occuring mutation
D379P
naturally occuring mutation
D379S
naturally occuring mutation
D379V
naturally occuring mutation
D379W
naturally occuring mutation
F590C
naturally occuring mutation
F590G
naturally occuring mutation
F590L
naturally occuring mutation
F590N
naturally occuring mutation
F590R
naturally occuring mutation
G116N
naturally occuring mutation
G116S
naturally occuring mutation
K251D
naturally occuring mutation
K251E
naturally occuring mutation
K251N
naturally occuring mutation
K251P
naturally occuring mutation
K251T
naturally occuring mutation
M354C
naturally occuring mutation
M354K
naturally occuring mutation
M354V
naturally occuring mutation
P192A
naturally occuring mutation
P192E
naturally occuring mutation
P192L
naturally occuring mutation
P192Q
naturally occuring mutation
P192R
naturally occuring mutation
P192S
naturally occuring mutation
P192V
naturally occuring mutation
P192W
naturally occuring mutation
P192Y
naturally occuring mutation
V583A
naturally occuring mutation
V583C
naturally occuring mutation
V583N
naturally occuring mutation
V583Y
naturally occuring mutation
V99M
naturally occuring mutation
W586A
naturally occuring mutation
W586C
naturally occuring mutation
W586E
naturally occuring mutation
W586G
naturally occuring mutation
W586H
naturally occuring mutation
W586I
naturally occuring mutation
W586K
naturally occuring mutation
W586L
naturally occuring mutation
W586N
naturally occuring mutation
W586S
naturally occuring mutation
W586V
naturally occuring mutation
F204A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H181A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H205A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
H219A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
K218A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
L177A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
L222A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
P206A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
R216A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
S212A
-
site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and S-200 HR gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of enzyme from small and catalytic subunit each overexpressed in Escherichia coli and purified. Small subunit protein stimulates catalytic subunit up to 7fold and confers upon it sensitivity to inhibition by valine
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
AHAS is the target of the sulfonylurea and imidazolinone herbicides
synthesis
construction of isobutanol production systems by overexpression of effective 2-oxoacid decarboxylase KivD and combinatorial overexpression of valine biosynthetic enzymes in Saccharomyces cerevisiae D452-2. Isobutanol production by the engineered strain is assessed in micro-aerobic batch fermentations using glucose as a sole carbon source, leading to production of 93 mg/l isobutanol, which corresponds to a fourfold improvement as compared with the control strain. Isobutanol production is further enhanced to 151 mg/l by additional overexpression of acetolactate synthase Ilv2p, acetohydroxyacid reductoisomerase Ilv5p, and dihydroxyacid dehydratase Ilv3p in the cytosol
brewing
-
unpleasant butterscotch-like flavor in beer due to accumulation of 2,3-butanedione derives from accumulation of mitochondrial matrix-targeted acetohydroxyacid synthase Ilv2 preprotein in the cytosol. Ilv2 preprotein accumulates in the cytosol of petite yeasts. Expression of a mutant allele of the gamma-subunit of the F1-ATPase, ATP3-5, could be an attractive way to reduce diacetyl formation by petite strains
drug development
-
the enzyme is a target for drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryan, E.D.; Kohlhaw, G.B.
Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast
J. Bacteriol.
120
631-637
1974
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Poulsen, C.; Stougaard, P.
Purification and properties of Saccharomyces cerevisiae acetolactate synthase from recombinant Escherichia coli
Eur. J. Biochem.
185
433-439
1989
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Pang, S.S.; Duggleby, R.G.
Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase
Biochemistry
38
5222-5231
1999
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lee, Y.T.; Duggleby, R.G.
Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP
Biochem. J.
395
331-336
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team
McCourt, J.A.; Duggleby, R.G.
How an enzyme answers multiple-choice questions
Trends Biochem. Sci.
30
222-225
2005
Escherichia coli, Saccharomyces cerevisiae (P07342)
Manually annotated by BRENDA team
He, Y.Z.; Li, Y.X.; Zhu, X.L.; Xi, Z.; Niu, C.; Wan, J.; Zhang, L.; Yang, G.F.
Rational design based on bioactive conformation analysis of pyrimidinylbenzoates as acetohydroxyacid synthase inhibitors by integrating molecular docking, CoMFA, CoMSIA, and DFT calculations
J. Chem. Inf. Model.
47
2335-2344
2007
Saccharomyces cerevisiae (P07342)
Manually annotated by BRENDA team
Kingsbury, J.M.; McCusker, J.H.
Cytocidal amino acid starvation of Saccharomyces cerevisiae and Candida albicans acetolactate synthase (ilv2{Delta}) mutants is influenced by the carbon source and rapamycin
Microbiology
156
929-939
2009
Saccharomyces cerevisiae, Candida albicans
Manually annotated by BRENDA team
Duggleby, R.G.; McCourt, J.A.; Guddat, L.W.
Structure and mechanism of inhibition of plant acetohydroxyacid synthase
Plant Physiol. Biochem.
46
309-324
2008
Arabidopsis thaliana, Brassica napus, Escherichia coli, Helianthus annuus, Nicotiana tabacum, Nitrosomonas europaea, Salmonella enterica subsp. enterica serovar Typhimurium, Thermotoga maritima, Saccharomyces cerevisiae (P07342), Gossypium hirsutum (Q42768)
Manually annotated by BRENDA team
Dasari, S.; Koelling, R.
Cytosolic localization of acetohydroxyacid synthase Ilv2 and its impact on diacetyl formation during beer fermentation
Appl. Environ. Microbiol.
77
727-731
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gokhale, K.; Tilak, B.
Mechanisms of bacterial acetohydroxyacid synthase (AHAS) and specific inhibitors of Mycobacterium tuberculosis AHAS as potential drug candidates against tuberculosis
Curr. Drug Targets
16
689-699
2015
Saccharomyces cerevisiae, Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WG41 and P9WKJ3), Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (P00892 and P0ADG1), Escherichia coli (P00893 and P00894), Escherichia coli (P08142 and P0ADF8), Mycobacterium tuberculosis H37Rv (P9WG41 and P9WKJ3)
Manually annotated by BRENDA team
Lee, W.; Seo, S.; Bae, Y.; Nan, H.; Jin, Y.; Seo, J.
Isobutanol production in engineered Saccharomyces cerevisiae by overexpression of 2-ketoisovalerate decarboxylase and valine biosynthetic enzymes
Bioprocess Biosyst. Eng.
35
1467-1475
2012
Saccharomyces cerevisiae (P07342), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lonhienne, T.; Garcia, M.D.; Guddat, L.W.
The role of a FAD cofactor in the regulation of acetohydroxyacid synthase by redox signaling molecules
J. Biol. Chem.
292
5101-5109
2017
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lonhienne, T.; Garcia, M.; Noble, C.; Harmer, J.; Fraser, J.; Williams, C.; Guddat, L.
High resolution crystal structures of the acetohydroxyacid synthase-pyruvate complex provide new insights into its catalytic mechanism
ChemistrySelect
2
11981-11988
2017
Saccharomyces cerevisiae (P07342)
-
Manually annotated by BRENDA team
Garcia, M.D.; Wang, J.G.; Lonhienne, T.; Guddat, L.W.
Crystal structure of plant acetohydroxyacid synthase, the target for several commercial herbicides
FEBS J.
284
2037-2051
2017
Saccharomyces cerevisiae, Arabidopsis thaliana (P17597), Arabidopsis thaliana
Manually annotated by BRENDA team
Lonhienne, T.; Garcia, M.D.; Pierens, G.; Mobli, M.; Nouwens, A.; Guddat, L.W.
Structural insights into the mechanism of inhibition of AHAS by herbicides
Proc. Natl. Acad. Sci. USA
115
E1945-E1954
2018
Saccharomyces cerevisiae (P07342), Arabidopsis thaliana (P17597)
Manually annotated by BRENDA team