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Information on EC 1.1.1.86 - ketol-acid reductoisomerase (NADP+)
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1.1.1.86 ketol-acid reductoisomerase (NADP+)IUBMB Comments
Also catalyses the reduction of 2-ethyl-2-hydroxy-3-oxobutanoate to 2,3-dihydroxy-3-methylpentanoate. The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382, ketol-acid reductoisomerase (NAD+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]).
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Word Map
- 1.1.1.86
-
branched-chain
- 5-phosphate
-
karis
- 1-deoxy-d-xylulose
- fosmidomycin
-
isoprenoids
- methylerythritol
- 1-deoxy-d-xylulose-5-phosphate
- deoxyxylulose
- l-valine
- isobutanol
-
non-mevalonate
-
2-c-methyl-d-erythritol
-
2-keto
-
dihydroxyacid
- 2-ketoisovalerate
-
isoleucine-valine
- drug development
- biofuel production
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
reductoisomerase, ketol-acid reductoisomerase, acetohydroxy acid isomeroreductase, ilv5p, isomeroreductase, acetohydroxyacid isomeroreductase, ahair, acetohydroxy acid reductoisomerase, ilvc1, acetolactate reductoisomerase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetohydroxy acid isomeroreductase
acetohydroxyacid isomeroreductase
AHAIR
AHIR
ilvC
IlvC1
IlvC2
KARI
ketol-acid reductoisomerase
acetohydroxyacid isomeroreductase
-
acetohydroxyacid isomeroreductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
active site structure
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
bifunctional enzyme that catalyses two different reactions at a common active site, an isomerization consisting of an alkyl migration, followed by an NADPH-dependent reduction of a-ketoacid
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
catalytic mechanism, overview
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
active site structure and catalytic mechanism, mechanism of induced fit, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(R)-2,3-dihydroxy-3-methylbutanoate:NADP+ oxidoreductase (isomerizing)
Also catalyses the reduction of 2-ethyl-2-hydroxy-3-oxobutanoate to 2,3-dihydroxy-3-methylpentanoate. The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382, ketol-acid reductoisomerase (NAD+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]).
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CAS REGISTRY NUMBER
COMMENTARY
9075-02-9
-
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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
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH
-
the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview
-
?
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2-aceto-2-hydroxybutyrate + NADP+
(2R,3R)-2,3-dihydroxy-3-methylvalerate + NADPH + H+
-
-
r
2-aceto-2-hydroxybutyrate + NADPH + H+
2,3-dihydroxy-3-methylvalerate + NADP+
-
-
-
r
2-acetolactate + NADP+
(2R)-2,3-dihydroxy-3-isovalerate + NADPH + H+
-
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+ + H+
-
the enzyme is the second of the valine pathway
-
r
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethyl-butanoate + NADP+
-
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methyl-butanoate + NADP+
-
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethyl-butanoate + NADP+
-
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methyl-butanoate + NADP+
-
-
-
?
NADP+ + 3-hydroxy-3-methyl-2-oxobutanoate
NADPH + acetolactate
-
-
-
?
NADPH + 2-oxo-3-hydroxyisovalerate
NADP+ + alpha,beta-dihydroxyisovalerate
-
-
-
?
NADPH + alpha-aceto-alpha-hydroxybutyrate
NADP+ + ?
-
enzyme of isoleucine biosynthesis
-
?
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
r
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
conformational changes in a plant ketol-acid reductoisomerase upon Mg2+ and NADPH binding, overview
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
the enzyme performs a two-step reaction of an alkyl migration followed by an NADPH-dependent reduction rection
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
r
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
-
-
?
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
-
-
?
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
-
-
?
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
-
-
?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
r
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
2-aceto-2-hydroxybutyrate + NADPH
2,3-dihydroxy-3-methylvalerate + NADP+
-
-
-
?
2-aceto-2-hydroxybutyrate + NADPH
2,3-dihydroxy-3-methylvalerate + NADP+
-
the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview
-
?
2-aceto-2-hydroxybutyrate + NADPH + H+
? + NADP+
-
-
r
2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+ + H+
-
-
-
r
2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+ + H+
-
-
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
second common reaction in the biosynthesis of the branched chain amino acids
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of valine synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
not reversible at pH 7.5, reversible at pH 9-10
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
-
the enzyme is involved in biosynthesis of the branched chain amino acid isoleucine, pathway overview
-
?
2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
-
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
-
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
-
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
-
-
?
3-hydroxypyruvate + NADPH + H+
? + NADP+
-
-
r
acetolactate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
-
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
-
activity is 6-10times greater than that for 2-acetolactate
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
not reversible at pH 7.5, reversible at pH 9-10
-
?, r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
alpha-keto-beta-hydroxyisovalerate is not a free intermediate
-
?, r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
ordered reaction with NADPH and the acetohydroxy acid adding in that order, and dihydroxy acid released before NADP+. 4 mol of NADPH bind per mol of enzyme
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
-
-
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
-
-
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
-
-
?
additional information
?
-
-
the enzyme is involved in biosynthesis of branched amino acids valine, isoleucine, and leucine, pathway overview
-
?
additional information
?
-
-
the enzyme catalyses the second reaction in the biosynthesis of the branched-chain amino acids
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
?
additional information
?
-
-
structure-biological activity relationship, overview
-
?
additional information
?
-
-
structure-biological activity relationship, overview
-
?
additional information
?
-
KARI catalyzes two reactions: alkyl migration and reduction. Structure-function relationship, effects of ligand binding, MG2+ and NADPH, on the enzyme conformation, overview
-
?
additional information
?
-
-
KARI catalyzes two reactions: alkyl migration and reduction. Structure-function relationship, effects of ligand binding, MG2+ and NADPH, on the enzyme conformation, overview
-
?
additional information
?
-
-
enzyme expression is up-regulated in germinating cysts developing appressoria, which are important for interaction of pathogen and host plants tomato and potato
-
?
additional information
?
-
-
the enzyme is involved in biosynthesis of branched chain amino acids valine, isoleucine, and leucine, effects of KARI inhibition effects on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of 2-oxo-3-hydroxyisovalerate to 2-acetolactate
-
?
additional information
?
-
-
structure-biological activity relationship, overview
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2-aceto-2-hydroxybutyrate + NADPH
2,3-dihydroxy-3-methylvalerate + NADP+
-
-
-
-
?
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+ + H+
-
the enzyme is the second of the valine pathway
-
-
r
NADPH + alpha-aceto-alpha-hydroxybutyrate
NADP+ + ?
-
enzyme of isoleucine biosynthesis
-
-
?
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
-
r
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
-
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
-
-
r
2-aceto-2-hydroxybutyrate + NADPH + H+
? + NADP+
-
-
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
second common reaction in the biosynthesis of the branched chain amino acids
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of valine synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
not reversible at pH 7.5, reversible at pH 9-10
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
additional information
?
-
-
the enzyme is involved in biosynthesis of branched amino acids valine, isoleucine, and leucine, pathway overview
-
-
?
additional information
?
-
-
the enzyme catalyses the second reaction in the biosynthesis of the branched-chain amino acids
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
-
?
additional information
?
-
-
structure-biological activity relationship, overview
-
-
?
additional information
?
-
-
structure-biological activity relationship, overview
-
-
?
additional information
?
-
-
enzyme expression is up-regulated in germinating cysts developing appressoria, which are important for interaction of pathogen and host plants tomato and potato
-
-
?
additional information
?
-
-
the enzyme is involved in biosynthesis of branched chain amino acids valine, isoleucine, and leucine, effects of KARI inhibition effects on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
-
?
additional information
?
-
-
structure-biological activity relationship, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
4 mol of NADPH bind per mol of enzyme
NADPH
required, the majority of the NADP+ molecule binds to the N-domain of KARI with polar contacts with 11 residues, including W133, G134, S135, Q136, R162, S165, S167, S201, D202, Q205, and G254. There are also contacts with the C-domain, although these are much fewer and involve only the phosphoryl oxygen atoms and the oxygen and nitrogen atoms of the nicotinamide group in NADPH, forming contacts with C517, S518, and T519, and with R589 in the polypeptide
NADPH
binding of NADPH is enthalpy driven. NADPH binding may have an opposing effect to that of Mg2+ binding by inducing an increase in structural stability
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
-
with acetolactate as substrate , Mg2+ is the only divalent metal ion that supports enzyme catalysis
Mg2+
the coordination geometry for Mg(1) is approximately octahedral, with three water ligands and three protein ligands, the carboxylate groups of D217, E389 and E393. Mg(2) is seven coordinate with six waters and a carboxylate oxygen from D217. A dissociation constant of about 500 microM applies to the interaction of Mg2+ with unliganded enzyme. In presence of NADPH the Kd increases to about 800 microM
Mg2+
required for the alkyl migration reaction, Km is 0.0072 mM, binding structure, overview
Mn2+
-
activates reaction with 3-hydroxy-3-methyl-2-oxobutanoate, no effect on reaction with acetolactate
additional information
-
Mn2+, Co2+, Ni2+, Zn2+, Ca2+, Cu2+ and Co3+ can not substitute for Mg2+
additional information
-
Mn2+, Co2+, Ni2+, Zn2+, Ca2+, Cu2+ and Co3+ can not substitute for Mg2+
additional information
the enzyme catalyzes a two-step reaction: an alkyl migration that requires Mg2+, and a reduction reaction involving NADPH. For the reduction reaction, a divalent metal ion is also required, with any of Mg2+, Mn2+, Co2+, or Ni2+ utilized in this role
additional information
-
the enzyme catalyzes a two-step reaction: an alkyl migration that requires Mg2+, and a reduction reaction involving NADPH. For the reduction reaction, a divalent metal ion is also required, with any of Mg2+, Mn2+, Co2+, or Ni2+ utilized in this role
additional information
-
the NADPH reaction step requires a divalent cation, e.g. Mg2+, Mn2+, or Co2+, but in a non-specific manner
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1-cyclopropanedicarboxylic acid
-
i.e. CPCA, inhibition in vivo, effect on pea root length, shoot length, and fermentative metabolism, effects of KARI inhibition effects on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
1-cyano-N-(2,4,5-trichlorophenyl)cyclopropanecarboxamide
-
inhibition rate: 0%
1-cyano-N-(2,4-dichlorophenyl)cyclopropanecarboxamide
-
inhibition rate: 97.04%
1-cyano-N-(2-hydroxyethyl)cyclopropanecarboxamide
-
inhibition rate: 98.92%
1-cyano-N-(4-methoxyphenyl)cyclopropanecarboxamide
-
inhibition rate: 3.95%
1-cyano-N-(4-methylphenyl)cyclopropanecarboxamide
-
inhibition rate: 61.21%
1-cyano-N-[(E)-(3,3-dichloroprop-1-yn-1-yl)diazenyl]sulfanylcyclopropanecarboxamide
-
inhibition rate: 100%
1-cyano-N-[2-(trifluoromethyl)phenyl]cyclopropanecarboxamide
-
inhibition rate: 0%
1-cyano-N-[3-(trifluoromethyl)phenyl]cyclopropanecarboxamide
-
inhibition rate: 0%
1-cyano-N-[4-(trifluoromethyl)phenyl]cyclopropanecarboxamide
-
inhibition rate: 0%
1-cyano-N-[[(3-methylcyclopropa-1,2-dien-1-yl)amino]sulfanyl]cyclopropanecarboxamide
-
inhibition rate: 69.81%
2,3-dihydroxy-3-methylbutanoic acid
-
linear noncompetitive inhibitor of both 2-acetolactate and NADPH
2-Hydroxy-2-methylbutyrate
-
0.01 M 45% inhibition
2-Hydroxybutyrate
-
0.01 M, 48% inhibition
2-Oxo-3-hydroxyisovalerate
-
0.001 mM, 58% inhibition
2-oxoisovalerate
-
0.01 M, 21% inhibition
ascorbic acid
-
slight inhibition with 2-acetolactate as substrate
L-ascorbic acid
-
slightly inhibitory with alpha-acetolactate as substrate
Mn2+
-
with acetolactate as substrate, Mn2+ behaves as a competitive inhibitor in presence of Mg2+
N'-(5-(3-pyridinyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N-(4-chlorophenyl)-1-cyanocyclopropanecarboxamide
-
inhibition rate: 93.92%
2-(4-benzylpiperazin-1-yl)-N-(3,4-dichlorophenyl)acetamide
-
72.6% inhibition at 100 microg/ml
2-(4-benzylpiperazin-1-yl)-N-(3,4-dichlorophenyl)acetamide
-
28.3% inhibition at 100 microg/ml
2-(4-benzylpiperazin-1-yl)-N-(3,4-dichlorophenyl)acetamide
-
48.1% inhibition at 200 microg/ml
2-dimethylphosphinoyl-2-hydroxyacetate
-
i.e. Hoe 704, potent competitive inhibitor in vitro but weak in vivo
2-dimethylphosphinoyl-2-hydroxyacetate
-
i.e. Hoe 704, potent competitive inhibitor in vitro but weak in vivo
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
nearly irreversible; reversible, strong competitive inhibition
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
i.e. HOE 704, inhibition in vivo, effect on pea root length, shoot length, and fermentative metabolism, effects of KARI inhibition on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
nearly irreversible; reversible, strong competitive inhibition
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
nearly irreversible; reversible, strong competitive inhibition
2-Hydroxyisovalerate
-
0.01 M, 38% inhibition
2-Hydroxyisovalerate
-
noncompetitive
2-Methyllactate
-
0.001 M, 61% inhibition; competitive
2-[[(4-methoxyphenyl)carbonyl]amino]benzoic acid
-
52% inhibition at 100 microg/ml
2-[[(4-methoxyphenyl)carbonyl]amino]benzoic acid
-
25.9% inhibition at 100 microg/ml
2-[[(4-methoxyphenyl)carbonyl]amino]benzoic acid
-
57.4% inhibition at 200 microg/ml
4,4'-(pentamethylenedioxy)dibenzamidne bis(2-hydroxyethanesulfonate)
-
binding structure and inhibition mechanism, overview
4,4'-(pentamethylenedioxy)dibenzamidne bis(2-hydroxyethanesulfonate)
-
binding structure and inhibition mechanism, overview
cyclopropane-1,1-dicarboxylate
a competitive slow-, tight-binding inhibitor
HOE 704
-
i.e. 2-dimethylphosphinoyl-2-hydroxyacetic acid, competitive inhibitor, potent in vitro, weak as in vivo herbicide
HOE 704
-
i.e. 2-dimethylphosphinoyl-2-hydroxyacetic acid, competitive inhibitor, potent in vitro, weak as in vivo herbicide
HOE 704
-
i.e. 2-dimethylphosphinoyl-2-hydroxyacetic acid, competitive inhibitor, potent in vitro, weak as in vivo herbicide
HOE 704
-
i.e. 2-dimethylphosphinoyl-2-hydroxyacetic acid, competitive inhibitor, potent in vitro, weak as in vivo herbicide
HOE 704
-
i.e. 2-dimethylphosphinoyl-2-hydroxyacetic acid, competitive inhibitor, potent in vitro, weak as in vivo herbicide
IpOHA
-
competitive inhibitor, potent in vitro, weak as in vivo herbicide
IpOHA
-
competitive inhibitor, potent in vitro, weak as in vivo herbicide
IpOHA
-
competitive inhibitor, potent in vitro, weak as in vivo herbicide
IpOHA
-
competitive inhibitor, potent in vitro, weak as in vivo herbicide
N-Hydroxy-N-isopropyloxamate
-
very strong, nearly irreversible inhibition, inhibition also with N-alkyl substituted derivates, tightest binding in presence of Mg2+ and NADPH
N-Hydroxy-N-isopropyloxamate
-
nearly irreversible, competitive; nearly irreversible, poor herbicidal action
N-Hydroxy-N-isopropyloxamate
-
i.e. IpOHA, potent competitive inhibitor in vitro but weak in vivo
N-Hydroxy-N-isopropyloxamate
-
nearly irreversible, competitive; nearly irreversible, poor herbicidal action
N-Hydroxy-N-isopropyloxamate
-
nearly irreversible, competitive; nearly irreversible, poor herbicidal action
N-Hydroxy-N-isopropyloxamate
-
i.e. IpOHA, potent competitive inhibitor in vitro but weak in vivo
NADP+
-
linear non-competitive with respect to 2-acetolactate, linear competitive inhibitor of NADPH
additional information
-
herbicidal effect of inhibitors, overview
-
additional information
no inhibition by 1-aminocyclopropanecarboxylate, 1-methylcyclopropanecarboxylate, 2-methylcyclopropanecarboxylate, cyclopropane-1,2-dicarboxylate, and cyclopropanecarboxylate dimethyl ester
-
additional information
-
no inhibition by N'-(5-methyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea, N'-(5-ethyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea, and N'-(5-propyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea; structure-activity relationship
-
additional information
-
high throughput receptor-based virtual screening of the ZINC/drug like database based on the crystal structure of ketol-acid reductoisomerase/N-hydroxy-N-isopropyloxamate complex, PDB entry 1YVE
-
additional information
-
molecular design of KARI inhibitors, and synthesis, overview. Structure-function relationship, analysis by computational docking of inhibitor molecules to cyrstal structure. No inhibition by 5-[(4-morpholino/piperidin-1-yl)acetyl]-10
-
additional information
-
no inhibition with p-mercuribenzoate, cysteine, 2-mercaptoethanol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
5 mM, enhances activity 2-hydroxy-2-ethyl-3-oxobutanoate as substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
2-aceto-2-hydroxybutanoate
-
pH 8.2, 30°C, chimeric enzyme Aabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli
0.04
(S)-2-acetolactate
mutant enzyme T84S, with NADH as cosubstrate, at pH 7.0 and 50°C
0.08
(S)-2-acetolactate
wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C
0.15
(S)-2-acetolactate
mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C
0.24
(S)-2-acetolactate
wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C
0.78
2-aceto-2-hydroxybutyrate
-
30°C
0.29
2-acetolactate
-
30°C, with 2-acetolactate or 2-aceto-2-hydroxybutyrate as substrate
0.026
NADH
mutant G50D/S52D, pH not specified in the publication, temperature not specified in the publication
0.027
NADH
mutant R48P/S51L/S52D/R84A, pH not specified in the publication, temperature not specified in the publication
0.028
NADH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.043
NADH
mutant R48P/S51L/S52D, pH not specified in the publication, temperature not specified in the publication
0.059
NADH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0089
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K69L
0.0112
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K75Q
0.029
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R68Q
0.072
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R76Q
0.007
NADPH
-
pH 8.2, 30°C, chimeric enzyme Arabidopsis thaliana acetohydroxy acid synthase is genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli
0.015
NADPH
-
30°C with 2-acetolactate or 2-aceto-2-hydroxybutyrate as substrate
0.0173
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.018
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0245
NADPH
-
pH 8.0, 22°C, reaction with 2-acetolactate, mutant enzyme R68QL
0.0365
NADPH
-
pH 8.0, 22°C, reaction with 2-acetolactate, mutant enzyme R76Q
0.08
NADPH
mutant G50D/S52D, pH not specified in the publication, temperature not specified in the publication
1
NADPH
mutant R48P/S51L/S52D, pH not specified in the publication, temperature not specified in the publication
1
NADPH
mutant R48P/S51L/S52D/R84A, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
78.3
2-aceto-2-hydroxybutyrate
-
30°C
0.77
(S)-2-acetolactate
wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C
1.09
(S)-2-acetolactate
wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C
1.3
(S)-2-acetolactate
mutant enzyme T84S, with NADH as cosubstrate, at pH 7.0 and 50°C
3.81
(S)-2-acetolactate
mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C
1.2
2-acetolactate
-
at pH 8.0, temperature not specified in the publication
26
3-hydroxypyruvate
-
at pH 8.0, temperature not specified in the publication
0.03
NADH
mutant R48P/S51L/S52D/R84A, pH not specified in the publication, temperature not specified in the publication
0.032
NADH
mutant R48P/S51L/S52D, pH not specified in the publication, temperature not specified in the publication
0.0883
NADH
-
pH 8, 22°C, mutant enzyme R68D/K69L/K75V/R76D and mutant enzyme R76D
0.15
NADH
mutant G50D/S52D, pH not specified in the publication, temperature not specified in the publication
0.26
NADH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.3
NADH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.00015
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R68Q
0.0002
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R76Q
0.000317
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K69L
0.000667
NADP+
-
pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K75Q
0.0000933
NADPH
-
pH 8.0, 22°C, reaction with acetolactate, mutant enzyme K75Q
0.004
NADPH
mutant G50D/S52D, pH not specified in the publication, temperature not specified in the publication
0.00617
NADPH
-
pH 8.0, 22°C, reaction with acetolactate, mutant enzyme R76Q
0.00667
NADPH
-
pH 8.0, 22°C, reaction with acetolactate, mutant enzyme R68Q
0.01
NADPH
mutant R48P/S51L/S52D/R84A, pH not specified in the publication, temperature not specified in the publication
0.013
NADPH
mutant R48P/S51L/S52D, pH not specified in the publication, temperature not specified in the publication
0.66
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.7
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.6
(S)-2-acetolactate
wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C
10.2
(S)-2-acetolactate
wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C
25.9
(S)-2-acetolactate
mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C
34.1
(S)-2-acetolactate
mutant enzyme T84S, with NADH as cosubstrate, at pH 7.0 and 50°C
2.4
2-acetolactate
-
at pH 8.0, temperature not specified in the publication
3.3
3-hydroxypyruvate
-
at pH 8.0, temperature not specified in the publication
4.16
3-hydroxypyruvate
-
at pH 8.0, temperature not specified in the publication
0.0046
NADH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0062
NADH
mutant G50D/S52D, pH not specified in the publication, temperature not specified in the publication