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Information on EC 1.1.1.86 - ketol-acid reductoisomerase (NADP+)
for references in articles please use BRENDA:EC1.1.1.86
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
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)+]).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.1.1.86
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branched-chain
- 5-phosphate
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karis
- 1-deoxy-d-xylulose
- fosmidomycin
-
isoprenoids
- methylerythritol
- 1-deoxy-d-xylulose-5-phosphate
- deoxyxylulose
- l-valine
- isobutanol
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2-c-methyl-d-erythritol
-
non-mevalonate
-
dihydroxyacid
-
2-keto
-
isoleucine-valine
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ilvbnce
- drug development
- biofuel production
- industry
Reaction Schemes
showSynonyms
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
2-hydroxy-3-keto acid reductoisomerase
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-
-
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acetohydroxy acid isomeroreductase
acetohydroxy acid reductoisomerase
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-
-
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acetohydroxy-acid isomeroreductase
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-
-
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acetohydroxy-acid reductoisomerase
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-
-
-
acetohydroxyacid isomeroreductase
acetolactate reductoisomerase
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-
-
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AHAIR
AHIR
alpha-keto-beta-hydroxylacil reductoisomerase
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-
-
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alpha-keto-beta-hydroxylacyl reductoisomerase
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-
-
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dehydrogenase, dihydroxyisovalerate (isomerizing)
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-
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dihydroxyisovalerate dehydrogenase (isomerizing)
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-
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EC 1.1.1.89
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formerly
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ilvC
IlvC1
IlvC2
isomerase, ketol acid reducto-
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-
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isomeroreductase
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-
-
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KARI
ketol-acid reductoisomerase
reductoisomerase
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-
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acetohydroxy acid isomeroreductase
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-
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acetohydroxyacid isomeroreductase
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KARI
-
-
-
-
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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+
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-
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(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
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(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
active site structure
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(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
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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rearrangement
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redox reaction
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
L-isoleucine biosynthesis I (from threonine), L-isoleucine biosynthesis III, L-valine biosynthesis, pyruvate fermentation to isobutanol (engineered)
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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
LITERATURE
COMMENTARY
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
-
Substrates: the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview
Products: -
Products: -
?
(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+
Substrates: -
Products: -
Products: -
r
2-aceto-2-hydroxybutyrate + NADPH + H+
2,3-dihydroxy-3-methylvalerate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-acetolactate + NADP+
(2R)-2,3-dihydroxy-3-isovalerate + NADPH + H+
Substrates: -
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+ + H+
-
Substrates: the enzyme is the second of the valine pathway
Products: -
Products: -
r
2-acetolactate + NADPH
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-glutaryl lactic acid + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethyl-butanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methyl-butanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-trichloromethyl acetolactic acid + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethyl-butanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methyl-butanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
acetolactate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
r
NADP+ + 3-hydroxy-3-methyl-2-oxobutanoate
NADPH + acetolactate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-oxo-3-hydroxyisovalerate
NADP+ + alpha,beta-dihydroxyisovalerate
-
Substrates: -
Products: -
Products: -
?
NADPH + alpha-aceto-alpha-hydroxybutyrate
NADP+ + ?
-
Substrates: enzyme of isoleucine biosynthesis
Products: -
Products: -
?
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(2S)-2-aceto-2-hydroxybutyrate + NADPH + H+
(R)-2,3-dihydroxy-3-methylvalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-aceto-2-hydroxybutyrate + NADPH + H+
(R)-2,3-dihydroxy-3-methylvalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH
Products: -
Products: -
?
(2S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH
(2R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH
(2R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxyisovalerate + NADP+
Substrates: the reaction includes the initial deprotonation of the substrate C2 hydroxy group, bridged by the two Mg2+ ions, alkyl migration from the C2-alkoxide carbon atom to the C3-carbon
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxyisovalerate + NADP+
Substrates: the reaction includes the initial deprotonation of the substrate C2 hydroxy group, bridged by the two Mg2+ ions, alkyl migration from the C2-alkoxide carbon atom to the C3-carbon
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
-
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
(2S)-2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
Substrates: conformational changes in a plant ketol-acid reductoisomerase upon Mg2+ and NADPH binding, overview
Products: -
Products: -
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
Substrates: the enzyme performs a two-step reaction of an alkyl migration followed by an NADPH-dependent reduction rection
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NAD+
Substrates: the enzyme can also use NADH for efficient catalysis. Higher activity by with NADPH as compared to NADH. kcat/Km ratio of NADH/NADPH is 0.051
Products: -
Products: -
?
(S)-2-acetolactate + NADH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NAD+
Substrates: the enzyme can also use NADH for efficient catalysis. Higher activity by with NADPH as compared to NADH. kcat/Km ratio of NADH/NADPH is 0.051
Products: -
Products: -
?
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: the enzyme can also use NADH for efficient catalysis. Higher activity by with NADPH as compared to NADH. kcat/Km ratio of NADH/NADPH is 0.051
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: the enzyme can also use NADH for efficient catalysis. Higher activity by with NADPH as compared to NADH. kcat/Km ratio of NADH/NADPH is 0.051
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: second enzyme in the branched-chain amino acid biosynthesis pathway
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: second enzyme in the branched-chain amino acid biosynthesis pathway
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-aceto-2-hydroxybutyrate + NADPH
2,3-dihydroxy-3-methylvalerate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-aceto-2-hydroxybutyrate + NADPH
2,3-dihydroxy-3-methylvalerate + NADP+
-
Substrates: the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview
Products: -
Products: -
?
2-aceto-2-hydroxybutyrate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
r
2-aceto-2-hydroxybutyrate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
r
2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+ + H+
-
Substrates: -
Products: -
Products: -
r
2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+ + H+
-
Substrates: -
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: second common reaction in the biosynthesis of the branched chain amino acids
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of valine synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: not reversible at pH 7.5, reversible at pH 9-10
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
-
Substrates: the enzyme is involved in biosynthesis of the branched chain amino acid isoleucine, pathway overview
Products: -
Products: -
?
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-ethyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-methylacetoacetate + NADPH + H+
3-hydroxy-2-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-tribromomethyl acetolactic acid + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
2-tribromomethyl acetolactic acid + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
2-trifluormethyl acetolactic acid + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
2-trifluormethyl acetolactic acid + NADPH
? + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-ethyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-ethylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
3-hydroxypyruvate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
r
3-hydroxypyruvate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
r
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
glycerate + NADP+
-
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
glycerate + NADP+
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
glycerate + NADP+
Substrates: -
Products: -
Products: -
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
-
Substrates: activity is 6-10times greater than that for 2-acetolactate
Products: -
Products: -
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: not reversible at pH 7.5, reversible at pH 9-10
Products: -
Products: -
r, ?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: alpha-keto-beta-hydroxyisovalerate is not a free intermediate
Products: -
Products: -
r, ?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: 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
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
Products: -
?
pyrroline-5-carboxylate + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
D6ERQ9, D6EC76
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
2-hydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in biosynthesis of branched amino acids valine, isoleucine, and leucine, pathway overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyses the second reaction in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-biological activity relationship, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-biological activity relationship, overview
Products: -
Products: -
?
additional information
?
-
Substrates: KARI catalyzes two reactions: alkyl migration and reduction. Structure-function relationship, effects of ligand binding, MG2+ and NADPH, on the enzyme conformation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: KARI catalyzes two reactions: alkyl migration and reduction. Structure-function relationship, effects of ligand binding, MG2+ and NADPH, on the enzyme conformation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-activity relationship
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme expression is up-regulated in germinating cysts developing appressoria, which are important for interaction of pathogen and host plants tomato and potato
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of 2-oxo-3-hydroxyisovalerate to 2-acetolactate
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-biological activity relationship, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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+
-
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+ + H+
-
Substrates: the enzyme is the second of the valine pathway
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
-
Substrates: -
Products: -
Products: -
?
NADPH + alpha-aceto-alpha-hydroxybutyrate
NADP+ + ?
-
Substrates: enzyme of isoleucine biosynthesis
Products: -
Products: -
?
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(2S)-2-acetolactate + NADPH
(2R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
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?
(2S)-2-acetolactate + NADPH
(2R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
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r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
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r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
Substrates: -
Products: -
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r
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
-
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: -
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: second enzyme in the branched-chain amino acid biosynthesis pathway
Products: -
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?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: second enzyme in the branched-chain amino acid biosynthesis pathway
Products: -
Products: -
?
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
Substrates: -
Products: -
Products: -
r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-aceto-2-hydroxybutyrate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
r
2-aceto-2-hydroxybutyrate + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
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r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: second common reaction in the biosynthesis of the branched chain amino acids
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Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of valine synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: not reversible at pH 7.5, reversible at pH 9-10
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
Substrates: enzyme of branched chain amino acid synthesis
Products: -
Products: -
r
2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
2-acetolactate + NADPH + H+
3-hydroxy-3-methyl-2-oxobutyrate + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in biosynthesis of branched amino acids valine, isoleucine, and leucine, pathway overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyses the second reaction in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-biological activity relationship, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-biological activity relationship, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme expression is up-regulated in germinating cysts developing appressoria, which are important for interaction of pathogen and host plants tomato and potato
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of the branched-chain amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-biological activity relationship, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
higher activity by with NADPH as compared to NADH. kcat/Km ratio of NADH/NADPH is 0.051
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
NADPH
the enzyme prefers NADPH as a cofactor rather than NADH. kcat/Km for NADPH is 322fold higher than kcat/KM for NADH
NADPH
higher activity by with NADPH as compared to NADH. kcat/Km ratio of NADH/NADPH is 0.051
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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+
two magnesium ions are located deep in the active site pocket and are separated by 4.7 A. The side chains of D188 and E192, and four water molecules form ligands with one of the Mg2+ ions, Mg2+(I), and the second Mg2+ ion, Mg2+ (II), is liganded also by the side-chain of D188, in addition to E224 and E228 and three water molecules
Mg2+
required for the alkyl migration reaction, Km is 0.0072 mM, binding structure, overview
Mg2+
the enzyme binds two Mg2+ ions in the active site to bridge the substrate ligand and protein. The substrate binding and catalytic efficiency of KARI are highly dependent on the Mg2+ concentration
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 NADPH reaction step requires a divalent cation, e.g. Mg2+, Mn2+, or Co2+, but in a non-specific manner
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((4-methoxyphenyl)carbamoyl) (5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl)amide
-
(2E)-1-[(2-fluorophenyl)(imino)methyl]-2-[(4-fluorophenyl)methylidene]-N-[(piperazin-1-yl)methyl]hydrazine-1-carbothioamide
0.2 mM, 82.04% inhibition
(2E)-1-[(2-fluorophenyl)(imino)methyl]-2-[(4-fluorophenyl)methylidene]-N-[[4-(4-methylpyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 9.89% inhibition
(2E)-1-[(2-fluorophenyl)(imino)methyl]-2-[(4-fluorophenyl)methylidene]-N-[[4-(pyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 11.75% inhibition
(2E)-1-[(2-fluorophenyl)(imino)methyl]-N-[(piperazin-1-yl)methyl]-2-[[4-(trifluoromethyl)phenyl]methylidene]hydrazine-1-carbothioamide
0.2 mM, 69.3% inhibition
(2E)-1-[(2-fluorophenyl)(imino)methyl]-N-[[4-(pyrimidin-2-yl)piperazin-1-yl]methyl]-2-[[4-(trifluoromethyl)phenyl]methylidene]hydrazine-1-carbothioamide
0.2 mM, 1.17% inhibition; 0.2 mM, 1.35% inhibition; 0.2 mM, 6.68% inhibition
(2E)-1-[imino(phenyl)methyl]-N-[[4-(4-methylpyrimidin-2-yl)piperazin-1-yl]methyl]-2-[[4-(trifluoromethyl)phenyl]methylidene]hydrazine-1-carbothioamide
0.2 mM, 12.27% inhibition; 0.2 mM, 61.99% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-1-[(2-fluorophenyl)(imino)methyl]-N-[(piperazin-1-yl)methyl]hydrazine-1-carbothioamide
0.2 mM, 74.8% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-1-[(2-fluorophenyl)(imino)methyl]-N-[[4-(4-methylpyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 11.94% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-1-[(2-fluorophenyl)(imino)methyl]-N-[[4-(pyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 14.91% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-1-[imino(3,4,5-trimethoxy-2-nitrophenyl)methyl]-N-[[4-(pyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 30.59% inhibition; 0.2 mM, 51.84% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-1-[imino(phenyl)methyl]-N-[(piperazin-1-yl)methyl]hydrazine-1-carbothioamide
0.2 mM, 60.45% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-1-[imino(phenyl)methyl]-N-[[4-(4-methylpyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 28.54% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-1-[imino(phenyl)methyl]-N-[[4-(pyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 7.4% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-N-[[4-(4,6-dimethylpyrimidin-2-yl)piperazin-1-yl]methyl]-1-[(2-fluorophenyl)(imino)methyl]hydrazine-1-carbothioamide
0.2 mM, 23.95% inhibition
(2E)-2-[(4-chlorophenyl)methylidene]-N-[[4-(4,6-dimethylpyrimidin-2-yl)piperazin-1-yl]methyl]-1-[imino(3,4,5-trimethoxy-2-nitrophenyl)methyl]hydrazine-1-carbothioamide
0.2 mM, 19.65% inhibition; 0.2 mM, 81.81% inhibition
(2E)-2-[(4-fluorophenyl)methylidene]-1-[imino(3,4,5-trimethoxy-2-nitrophenyl)methyl]-N-[[4-(4-methylpyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 7.72% inhibition
(2E)-2-[(4-fluorophenyl)methylidene]-1-[imino(3,4,5-trimethoxy-2-nitrophenyl)methyl]-N-[[4-(pyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 13.65% inhibition
(2E)-2-[(4-fluorophenyl)methylidene]-1-[imino(phenyl)methyl]-N-[(piperazin-1-yl)methyl]hydrazine-1-carbothioamide
0.2 mM, 72.01% inhibition
(2E)-2-[(4-fluorophenyl)methylidene]-1-[imino(phenyl)methyl]-N-[[4-(4-methylpyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 10.34% inhibition
(2E)-2-[(4-fluorophenyl)methylidene]-1-[imino(phenyl)methyl]-N-[[4-(pyrimidin-2-yl)piperazin-1-yl]methyl]hydrazine-1-carbothioamide
0.2 mM, 10.14% inhibition
(2E)-N-[[4-(4,6-dimethylpyrimidin-2-yl)piperazin-1-yl]methyl]-1-[(2-fluorophenyl)(imino)methyl]-2-[(4-fluorophenyl)methylidene]hydrazine-1-carbothioamide
0.2 mM, 75.66% inhibition
(2E)-N-[[4-(4,6-dimethylpyrimidin-2-yl)piperazin-1-yl]methyl]-2-[(4-fluorophenyl)methylidene]-1-[imino(3,4,5-trimethoxy-2-nitrophenyl)methyl]hydrazine-1-carbothioamide
0.2 mM, 6.22% inhibition; 0.2 mM, 78.38% inhibition
(2E)-N-[[4-(4,6-dimethylpyrimidin-2-yl)piperazin-1-yl]methyl]-2-[(4-fluorophenyl)methylidene]-1-[imino(phenyl)methyl]hydrazine-1-carbothioamide
0.2 mM, 8.19% inhibition
(E)-[6-(4-fluorophenyl)-2-sulfanylidene-1,6-dihydropyrimidin-5(2H)-ylidene](4-methylphenyl)methanolate
-
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
6-hydroxy-2-methylthiazolo[4,5-d]pyrimidine-5,7(4H,6H)-dione
NSC116565, potent time-dependent inhibitor. The inhibitor binds to Mycobacterium tuberculosis KARI in the presence and absence of the cofactor, NADPH. Inhibits the growth of Mycobacterium tuberculosis H37Ra strain with MIC50 value of 0.00293 mM; NSC116565, potent time-dependent inhibitor. The inhibitor binds to Mycobacterium tuberculosis KARI in the presence and absence of the cofactor, NADPH. Inhibits the growth of Mycobacterium tuberculosis H37Rv strain with MIC50 value of 0.00606 mM
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%
N-(4-chlorophenyl)-N'-[5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
low toxicity against HEK 293T cell lines
N-(4-methoxyphenyl)-N'-[5-(5-nitrofuran-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
low toxicity against HEK 293T cell lines
N-(4-methoxyphenyl)-N'-[5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
low toxicity against HEK 293T cell lines
N-[(4-methoxyphenyl)carbamoyl]-5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-aminide
-
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-dimethylphosphoryl-2-hydroxy-acetic acid
-
i.e. Hoe 704, reversible inhibitor
2-dimethylphosphoryl-2-hydroxy-acetic acid
i.e. Hoe 704, reversible inhibitor
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
cyclopropane-1,1-dicarboxylate
binds in a competitively and in multi-dentate manner to the enzyme; the compounds bind competitively and in multi-dentate manner to the enzyme
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
MMV553002
i.e. 3-((methylsulfonyl)methyl)-2H-benzo[b][1,4]oxazin-2-one
MMV553002
i.e. 3-((methylsulfonyl)methyl)-2H-benzo[b][1,4]oxazin-2-one
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
N-isopropyloxalyl hydroxamate
binds slowly to the enzyme, binds in a competitively and in multi-dentate manner to the enzyme. The observation that the inhibitor is processed to its deoxygenated form in crystallo provides an alternative explanation for the relatively weak herbicidal/antimicrobial activity affordsed by N-isopropyloxalyl hydroxamate despite its low Ki value; the compounds bind competitively and in multi-dentate manner to the enzyme. Binds slowly to the enzyme. Intact N-isopropyloxalyl hydroxamate is present in only 25% of binding sites, whereas its deoxygenated form is present in the remaining sites. This deoxy form of N-isopropyloxalyl hydroxamate binds rapidly to the enzyme, but with much weaker affinity (Ki: 0.021 mM)
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bacterial Infections
Discovery, Synthesis and Evaluation of a Ketol-Acid Reductoisomerase Inhibitor.
Malaria
A computational study of the molecular basis of antibiotic resistance in a DXR mutant.
Malaria
Molecular epidemiology of malaria in Cameroon. XXV. In vitro activity of fosmidomycin and its derivatives against fresh clinical isolates of Plasmodium falciparum and sequence analysis of 1-deoxy-D-xylulose 5-phosphate reductoisomerase.
Malaria
Synthesis and evaluation of alpha,beta-unsaturated alpha-aryl-substituted fosmidomycin analogues as DXR inhibitors.
Neoplasms
Discovery of a Pyrimidinedione Derivative with Potent Inhibitory Activity against Mycobacterium tuberculosis Ketol-Acid Reductoisomerase.
Otitis Externa
Differences in protein profiles between Malassezia pachydermatis strains obtained from healthy and infected dogs.
Tuberculosis
A computational study of the molecular basis of antibiotic resistance in a DXR mutant.
Tuberculosis
Analogues of the Herbicide, N-Hydroxy-N-isopropyloxamate, Inhibit Mycobacterium tuberculosis Ketol-Acid Reductoisomerase and Their Prodrugs Are Promising Anti-TB Drug Leads.
Tuberculosis
Biochemical and functional characterization of Mycobacterium tuberculosis ketol-acid reductoisomerase.
Tuberculosis
Biosynthesis of isoleucine & valine in Mycobacterium tuberculosis H 37 Rv. 3. Purification & properties of acetohydroxy acid isomeroreductase.
Tuberculosis
Crystal structure of Mycobacterium tuberculosis ketol-acid reductoisomerase at 1.0 Å resolution - a potential target for anti-tuberculosis drug discovery.
Tuberculosis
Design and development of ((4-methoxyphenyl)carbamoyl) (5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl)amide analogues as Mycobacterium tuberculosis ketol-acid reductoisomerase inhibitors.
Tuberculosis
Discovery and evaluation of novel Mycobacterium tuberculosis ketol-acid reductoisomerase inhibitors as therapeutic drug leads.
Tuberculosis
Discovery of a Pyrimidinedione Derivative with Potent Inhibitory Activity against Mycobacterium tuberculosis Ketol-Acid Reductoisomerase.
Tuberculosis
Discovery, Synthesis and Evaluation of a Ketol-Acid Reductoisomerase Inhibitor.
Tuberculosis
Kinetic and chemical mechanism of Mycobacterium tuberculosis 1-deoxy-D-xylulose-5-phosphate isomeroreductase.
Tuberculosis
Toward Mycobacterium tuberculosis DXR inhibitor design: homology modeling and molecular dynamics simulations.
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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
0.06
(S)-2-acetolactate
pH 8.0, 60°C, 10 mM Mg2+, cofactor: NADPH
0.074
(S)-2-acetolactate
pH 8.0, 37°C, 10 mM Mg2+, cofactor: NADPH
0.08
(S)-2-acetolactate
wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C
0.091
(S)-2-acetolactate
pH 8.0, 60°C, 6 mM Mg2+, cofactor: NADH
0.093
(S)-2-acetolactate
pH 8.0, 60°C, 2 mM Mg2+, cofactor: NADPH
0.099
(S)-2-acetolactate
pH 8.0, 37°C, 10 mM Mg2+, cofactor: NADH
0.14
(S)-2-acetolactate
pH 8.0, 25°C, 10 mM Mg2+, cofactor: NADPH
0.144
(S)-2-acetolactate
pH 8.0, 60°C, 2 mM Mg2+, cofactor: NADH
0.15
(S)-2-acetolactate
mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C
0.157
(S)-2-acetolactate
pH 8.0, 37°C, 2 mM Mg2+, cofactor: NADPH
0.165
(S)-2-acetolactate
pH 8.0, 37°C, 2 mM Mg2+, cofactor: NADH
0.184
(S)-2-acetolactate
pH 8.0, 25°C, 2 mM Mg2+, cofactor: NADPH
0.188
(S)-2-acetolactate
pH 8.0, 25°C, 10 mM Mg2+, cofactor: NADH
0.24
(S)-2-acetolactate
wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C
0.469
(S)-2-acetolactate
pH 8.0, 25°C, 2 mM Mg2+, cofactor: NADH
4.43
(S)-2-acetolactate
-
pH 7.5, 55°C, 5 mM Mg2+, cofactor: NADPH
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
0.011
(S)-2-acetolactate
-
pH 7.5, 55°C, 5 mM Mg2+, cofactor: NADH
0.013
(S)-2-acetolactate
-
pH 7.5, 55°C, 5 mM Mg2+, cofactor: NADPH
0.055
(S)-2-acetolactate
pH 8.0, 25°C, 2 mM Mg2+, cofactor: NADH
0.058
(S)-2-acetolactate
pH 8.0, 25°C, 2 mM Mg2+, cofactor: NADPH
0.06
(S)-2-acetolactate
pH 8.0, 25°C, 10 mM Mg2+, cofactor: NADH
0.068
(S)-2-acetolactate
pH 8.0, 25°C, 10 mM Mg2+, cofactor: NADPH
0.157
(S)-2-acetolactate
pH 8.0, 37°C, 2 mM Mg2+, cofactor: NADH
0.164
(S)-2-acetolactate
pH 8.0, 37°C, 10 mM Mg2+, cofactor: NADH
0.192
(S)-2-acetolactate
pH 8.0, 37°C, 2 mM Mg2+, cofactor: NADPH
0.195
(S)-2-acetolactate
pH 8.0, 37°C, 10 mM Mg2+, cofactor: NADPH
0.444
(S)-2-acetolactate
pH 8.0, 60°C, 6 mM Mg2+, cofactor: NADH
0.526
(S)-2-acetolactate
pH 8.0, 60°C, 2 mM Mg2+, cofactor: NADH
0.77
(S)-2-acetolactate
wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C
0.876
(S)-2-acetolactate
pH 8.0, 60°C, 10 mM Mg2+, cofactor: NADPH
0.957
(S)-2-acetolactate
pH 8.0, 60°C, 2 mM Mg2+, cofactor: NADPH
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
0.0029
(S)-2-acetolactate
-
pH 7.5, 55°C, 5 mM Mg2+, cofactor: NADPH
0.00383
(S)-2-acetolactate
-
pH 7.5, 55°C, 5 mM Mg2+, cofactor: NADH
0.12
(S)-2-acetolactate
pH 8.0, 25°C, 2 mM Mg2+, cofactor: NADH
0.32
(S)-2-acetolactate
pH 8.0, 25°C, 2 mM Mg2+, cofactor: NADPH
0.33
(S)-2-acetolactate
pH 8.0, 25°C, 10 mM Mg2+, cofactor: NADH
0.49
(S)-2-acetolactate
pH 8.0, 25°C, 10 mM Mg2+, cofactor: NADPH
0.95
(S)-2-acetolactate
pH 8.0, 37°C, 2 mM Mg2+, cofactor: NADH
1.23
(S)-2-acetolactate
pH 8.0, 37°C, 2 mM Mg2+, cofactor: NADPH
1.66
(S)-2-acetolactate
pH 8.0, 37°C, 10 mM Mg2+, cofactor: NADH
2.63
(S)-2-acetolactate
pH 8.0, 37°C, 10 mM Mg2+, cofactor: NADPH
3.66
(S)-2-acetolactate
pH 8.0, 60°C, 2 mM Mg2+, cofactor: NADH
4.6
(S)-2-acetolactate
wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C
4.88
(S)-2-acetolactate
pH 8.0, 60°C, 6 mM Mg2+, cofactor: NADH
10.2
(S)-2-acetolactate
wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C
10.3
(S)-2-acetolactate
pH 8.0, 60°C, 2 mM Mg2+, cofactor: NADPH
14.58
(S)-2-acetolactate
pH 8.0, 60°C, 10 mM Mg2+, cofactor: NADPH
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
0.7
NADH
mutant R48P/S51L/S52D, pH not specified in the publication, temperature not specified in the publication
1.1
NADH
mutant R48P/S51L/S52D/R84A, pH not specified in the publication, temperature not specified in the publication
9
NADH
wild-type, pH not specified in the publication, temperature not specified in the publication
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
0.043
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.05
NADPH
mutant G50D/S52D, pH not specified in the publication, temperature not specified in the publication
37
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00306
((4-methoxyphenyl)carbamoyl) (5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl)amide
pH 8.0, 25°C
0.00659
(2E)-1-[(2-fluorophenyl)(imino)methyl]-2-[(4-fluorophenyl)methylidene]-N-[(piperazin-1-yl)methyl]hydrazine-1-carbothioamide
pH and temperature not specified in the publication
0.00846
(2E)-1-[(2-fluorophenyl)(imino)methyl]-N-[(piperazin-1-yl)methyl]-2-[[4-(trifluoromethyl)phenyl]methylidene]hydrazine-1-carbothioamide
pH and temperature not specified in the publication
0.01975
(2E)-2-[(4-chlorophenyl)methylidene]-1-[(2-fluorophenyl)(imino)methyl]-N-[(piperazin-1-yl)methyl]hydrazine-1-carbothioamide
pH and temperature not specified in the publication
0.03519
(2E)-2-[(4-chlorophenyl)methylidene]-N-[[4-(4,6-dimethylpyrimidin-2-yl)piperazin-1-yl]methyl]-1-[imino(3,4,5-trimethoxy-2-nitrophenyl)methyl]hydrazine-1-carbothioamide
pH and temperature not specified in the publication
0.00038
(2E)-N-[[4-(4,6-dimethylpyrimidin-2-yl)piperazin-1-yl]methyl]-1-[(2-fluorophenyl)(imino)methyl]-2-[(4-fluorophenyl)methylidene]hydrazine-1-carbothioamide
pH and temperature not specified in the publication
0.00371
(E)-[6-(4-fluorophenyl)-2-sulfanylidene-1,6-dihydropyrimidin-5(2H)-ylidene](4-methylphenyl)methanolate
pH 8.0, 25°C
0.0203
1-aminocarbonylcyclopropanecarboxylate
pH 8.0, 30°C, recombinant enzyme
0.0585
1-cyano-cyclopropane-1-carboxylate
pH and temperature not specified in the publication
207.9
1-cyano-N-[[(E)-(3,3-dichloroprop-1-yn-1-yl)diazenyl]sulfanyl]cyclopropanecarboxamide
-
-
0.145
2,3-dihydroxy-3-isovalerate
-
pH 8.2, 30°C, (2S)-2-aceto-2-hydroxybutanoate as variable substrate, 0.250 mM NADPH as fixed substrate
0.00472 - 0.00835
N-(4-chlorophenyl)-N'-[5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
0.00202 - 0.00548
N-(4-methoxyphenyl)-N'-[5-(5-nitrofuran-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
0.00927
N-(4-methoxyphenyl)-N'-[5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
pH 8.0, 25°C
0.00306
N-[(4-methoxyphenyl)carbamoyl]-5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-aminide
pH 8.0, 25°C
0.095
2,3-dihydroxyisovalerate
-
pH 8.2, 30°C, (2S)-2-acetolactate as variable substrate, 0.250 mM NADPH as fixed substrate
0.935
2,3-dihydroxyisovalerate
-
pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate
1.5
2,3-dihydroxyisovalerate
-
pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-aceto-2-hydroxybutanoate as fixed substrate
0.00019
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
pH 7.5, 25°C, with 2-aceto-2-hydroxybutyrate as substrate
0.00046
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
pH 7.5, 25°C, with 2-acetolactate as substrate
0.0003
2-dimethylphosphoryl-2-hydroxy-acetic acid
pH 8.0, 25°C
0.24
2-hydroxy-2-methyl-3-oxopentanoate
-
pH 8.2, 30°C, (2S)-2-aceto-2-hydroxybutanoate as variable substrate, 0.075 mM NADPH as fixed substrate
0.245
2-hydroxy-2-methyl-3-oxopentanoate
-
pH 8.2, 30°C, (2S)-2-acetolactate as variable substrate, 0.075 mM NADPH as fixed substrate
1.7
2-hydroxy-2-methyl-3-oxopentanoate
-
pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate
3.6
2-hydroxy-2-methyl-3-oxopentanoate
-
pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-aceto-2-hydroxybutanoate as fixed substrate
0.0000903
cyclopropane-1,1-dicarboxylate
pH 8.0, 30°C, recombinant enzyme, versus hydroxypyruvate
0.00275
cyclopropane-1,1-dicarboxylate
pH and temperature not specified in the publication
0.0025
ethylene glycol
pH 8.0, 30°C, recombinant enzyme, competitive mode
0.0032
ethylene glycol
pH 8.0, 30°C, recombinant enzyme, uncompetitive mode
0.000153
MMV553002
pH 8.0, temperature not specified in the publication
0.000531
MMV553002
pH 8.0, temperature not specified in the publication
0.0000222
MMV688271
pH 8.0, temperature not specified in the publication
0.0000384
MMV688271
pH 8.0, temperature not specified in the publication
0.00472
N-(4-chlorophenyl)-N'-[5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
pH 8.0, 25°C
0.00835
N-(4-chlorophenyl)-N'-[5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
pH 8.0, 25°C
0.00202
N-(4-methoxyphenyl)-N'-[5-(5-nitrofuran-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
pH 8.0, 25°C
0.00548
N-(4-methoxyphenyl)-N'-[5-(5-nitrofuran-2-yl)-1,3,4-thiadiazol-2-yl]thiourea
pH 8.0, 25°C
0.0000079
N-isopropyloxalyl hydroxamate
pH 8.0, 25°C, intact N-isopropyloxalyl hydroxamate is present in only 25% of binding sites, whereas its deoxygenated form is present in the remaining sites. This deoxy form of N-isopropyloxalyl hydroxamate binds rapidly to the enzyme, but with much weaker affinity (Ki: 0.021 mM)
0.0000903
N-isopropyloxalyl hydroxamate
pH and temperature not specified in the publication
0.005
NADP+
-
pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate
0.0075
NADP+
-
pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-aceto-2-hydroxybutanoate as fixed substrate
0.225
NADP+
-
pH 8.2, 30°C, (2S)-2-aceto-2-hydroxybutanoate as variable substrate, 0.075 mM NADPH as fixed substrate
0.33
NADP+
-
pH 8.2, 30°C, (2S)-2-acetolactate as variable substrate, 0.075 mM NADPH as fixed substrate
additional information
1-cyano-N-(4-methylphenyl)cyclopropanecarboxamide
-
value above 300
additional information
additional information
-
-
-
additional information
additional information
inhibition mechanism and kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
1.9
additional information
-
the specific activity with pyruvate is 1% and with 2-ketovalerate, 2-ketopantoate and 2-ketobutyrate is 8% of that of 2-acetolactate, comparison of activities of wild-type and mutant enzymes
1.9
-
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.2
8.6
-
with 2-hydroxy-2-ethyl-3-oxobutanoate as substrate, Tris-HCl buffer, alpha-aceto-alpha-hydroxybutyrate as substrate, Tris buffer
9.4
-
reaction with 2,3-dihydroxyisovalerate
8.2
-
isomeroreductase activity of the chimeric enzyme composed of Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in Escherichia coli
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
pH 6.5: about 35% of maximal activity, pH 8.5: about 90% of maximal activity, reaction with 2-acetolactate, isoenzyme 1
6.6 - 8.8
-
pH 6.6: about 65% of maximal activity, pH 8.8: about 90% of maximal activity, reaction with 2-acetolactate, Tris buffer
6.8 - 8
-
pH 6.8: about 40% of maximal activity
7 - 10
pH 7.0: 87% of maximal activity, pH 10.0: 61% of maximal activity
7 - 8.5
7 - 9
-
pH 7.0: about 40% of maximal activity, pH 9.0: about 90% of maximal activity, with 2-hydroxy-2-ethyl-3-oxobutanoate as substrate, Tris-HCl buffer
7 - 8.5
-
pH 7.0: about 60% of maximal activity, pH 8.5: about 65% of maximal activity
7 - 8.5
-
pH 7.0: about 25% of maximal activity, pH 8.0-8.5: optimum, isoenzyme 1
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
60
the secondary structure of the enzyme remains intact in the presence of 2 mM Mg2+ at 60°C
65 - 95
the enzyme retains most of its native folding, when the temperature is increased to 65°C. At 95°C, the enzyme is completely unfolded
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
the enzyme exhibits pH-tolerance over a broader range (pH 3.0-8.0), which is preferred in industrial application
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a histatin-resistant derivative of Candida albicans strain 132A is used
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
ketol-acid reductoisomerase (Ilv5p), isocitrate lyase (Icl1p), fructose biphosphate aldolase (Fba1p) and pyruvate decarboxylase (Pdc2p) are present in the histatin-resistant derivative strain 132A but absent in the in the parent strain
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
metabolism
physiological function
drug target
the enzyme is a TB drug target and 6-hydroxy-2-methylthiazolo[4,5-d]pyrimidine-5,7(4H,6H)-dione (NSC116565) is a promising lead for anti-TB drug development
drug target
potential drug target for bacterial infections including Mycobacterium tuberculosis
drug target
the enzyme is present in bacteria but not in humans, making it an attractive proposition for drug discovery
drug target
potential drug target for bacterial infections including Mycobacterium tuberculosis
drug target
the enzyme is responsible for the second step of the biosynthesis of branched chain amino acids in plants and microorganisms and thus serves as a key inhibition target potentially without effects on mammals
drug target
-
the enzyme is present in bacteria but not in humans, making it an attractive proposition for drug discovery
-
drug target
-
the enzyme is responsible for the second step of the biosynthesis of branched chain amino acids in plants and microorganisms and thus serves as a key inhibition target potentially without effects on mammals
-
drug target
-
potential drug target for bacterial infections including Mycobacterium tuberculosis
-
metabolism
the enzyme is involved in the branched-chain amino acid biosynthesis pathway
metabolism
-
one of the key enzymes for the synthesis of branched-chain amino acids isoleucine, leucine and valine
metabolism
-
the enzyme catalyzes the first common step in biosynthesis of branched-chain amino acids isoleucine, leucine and valine
metabolism
the enzyme is involved in the branched-chain amino acid biosynthesis
metabolism
the enzyme is involved in the branched chain amino acid biosynthesis pathway
metabolism
the enzyme serves as a key inhibition target potentially without effects on mammals
metabolism
second enzyme in the branched chain amino acid biosynthesis pathway
metabolism
second enzyme in the branched-chain amino acid biosynthesis pathway
metabolism
second enzyme in the branched-chain amino acid pathway
metabolism
second enzyme in the branched-chain amino acid biosynthesis pathway
metabolism
the enzyme catalyzes the second step in the BCAA biosynthetic pathway
metabolism
-
the enzyme is involved in the branched-chain amino acid biosynthesis
metabolism
second enzyme in the branched-chain amino acid biosynthesis pathway
metabolism
-
the enzyme is involved in the branched chain amino acid biosynthesis pathway
-
metabolism
-
second enzyme in the branched-chain amino acid biosynthesis pathway
-
metabolism
-
second enzyme in the branched chain amino acid biosynthesis pathway
-
metabolism
-
second enzyme in the branched-chain amino acid pathway
-
metabolism
-
the enzyme serves as a key inhibition target potentially without effects on mammals
-
metabolism
-
second enzyme in the branched-chain amino acid biosynthesis pathway
-
metabolism
-
the enzyme is involved in the branched-chain amino acid biosynthesis
-
physiological function
the enzyme is responsible for the second step of the biosynthesis of branched chain amino acids in plants and microorganisms
physiological function
-
the enzyme is responsible for the second step of the biosynthesis of branched chain amino acids in plants and microorganisms
-
Show AA Sequence and Transmembrane Helices (19305 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000
120000
-
2 * 120000, Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in Escherichia coli, SDS-PAGE
205000
220000
240000
-
Arabidopsis 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, gel filtration
57000
59000
220000
-
sedimentation equilibrium centrifugation
57000
-
4 * 57000, equilibrium sedimentation after treatment with 0.1 M 2-mercaptoethanol and 6 M guanidine hydrochloride
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
homodimer
monomer
tetramer
dimer
structure-function relationship, effects of ligand, Mg2+ and NADPH, binding on the enzyme conformation, overview
dimer
-
2 * 120000, Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in Escherichia coli, SDS-PAGE
dodecamer
-
the dodecameric architecture is assembled by six dimeric units which are positioned on the tetrahedron edges to form a tetrahedron with T symmetry
tetramer
-
three-dimensional enzyme structure, subunit domain structures, surface contact and interlock, crystal structure analysis, overview
tetramer
-
4 * 57000, equilibrium sedimentation after treatment with 0.1 M 2-mercaptoethanol and 6 M guanidine hydrochloride
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1 M sodium potassium tartrate, 200 mM sodium chloride, 100 mM imidazole pH 8.0
hanging drop vapor diffusion method, using 0.25 M NaCl, 28% (w/v) polyethylene glycol 3350 and 0.1 M bis-Tris, pH 5.5
hanging-drop vapor-diffusion method at 20°C, crystal structure in complex with NADP+ and two Mg2+ ions at 2.6 A resolution
in complex with Mg2+ and NADPH at 2.3 A resolution. The binding of Mg2+ increases structural disorder while the binding of NADPH increases the structural rigidity of the enzyme. The binding of Mg2+ and NADPH opens the interface between the N- and C-domains, thereby allowing access for the substrates to bind
purified recombinant His-tagged enzyme, 9 mg/ml protein in 20 mM sodium HEPES, pH 7.5, and NADPH in a ratio of 10 mol NADPH per mol of enzyme, hanging drop vapour diffusion method, equal volumes of 0.003 ml of protein and reservoir solution, the latter containing 1.6 M ammonium sulfate, and 0.1 M sodium bicine, pH 9.0, 17°C, 6 months, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
hanging drop vapor diffusion method, using 0.1 M bis-Tris, pH 6.0, 22% (w/v) polyethylene glycol monomethylether 5000
in complex with NADPH and the transition state analogue N-isopropyloxamate and apo-form. The enzyme has a seven-residue specificity loop
native enzyme with two magnesium ions bound in the active site, hanging drop vapor diffusion method, using 250 mM MgCl2, 20% (w/v) PEG 3350, 100 mM Tris/HCl, pH 8.0
enzyme KARI in complex with Mg2+ or with Mg2+ and NADPH, hanging-drop method by vaporphase diffusion at 18°C, 0.003 ml of protein solution containing 6 mg/ml enzyme, 50 mM Hepes, pH 7.5, 5 mM NADPH, and 5 mM MgCl2, is mixed with 0.001 ml of reservoir solution containing 0.2 M magnesium chloride hexahydrate, 0.1 M Tris-HCl, pH 8.5, and 15% w/v PEG 4000, a few days to 3 months, X-ray diffraction structure determination and analysis at 1.55 A and 2.80 A resolution, respectively, molecular replacement
The dodecamer architecture of 23 point group symmetry is assembly of six dimeric units and dimerization is essential for the formation of the active site
-
ammonium sulfate precipitation, crystal structure of the enzyme complexed with NADPH, two magnesium ions and N-hydroxy-N-isopropyloxamate, a herbicidal transition state analog determined at 1.65 A resolution, recombinant enzyme overexpressed in Escherichia coli
-
crystal structures of the enzyme in complex with two transition state analogues, cyclopropane-1,1-dicarboxylate and N-isopropyloxalyl hydroxamate. Hanging-drop vapor-diffusion method
hanging drop method, cocrystallization of 3-((methylsulfonyl)methyl)-2H-benzo[b][1,4]oxazin-2-one in complex with the enzyme
hanging-drop vapor-diffusion method. Crystal structures of Staphylococcus aureus KARI in complex with two transition state analogues, cyclopropane-1,1-dicarboxylate and N-isopropyloxalyl hydroxamate
micro-batch and hanging-drop vapor-diffusion methods. The crystal structure is determined at 1.69 A resolution. The crystal structure of SpIlvC contains an asymmetric dimer in which one subunit is in apo-form and the other in NADP(H) and Mg2+-bound form
hanging drop vapor diffusion method, using 0.1 M bis-Tris, pH 5.0, 20% (w/v) w/v polyethylene glycol 1500
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R48P/S51L/S52D
mutant engineered for reversal in cofactor specificity for NADH over NADPH
R48P/S51L/S52D/R84A
mutant engineered for reversal in cofactor specificity for NADH over NADPH
D217E
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
D217N
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E213Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
E221D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E221Q
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E389D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E389Q
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E393D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E393Q
-
the mutant is insoluble, a soluble form is obtained only after denaturation
H132K
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
H132Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155E
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155R
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K69L
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 2.1fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 163 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is comparable to that of the wild-type emzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is 1.8fold higher than that of the wild-type enzyme
K75Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 2.7fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 77.5 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is lower by a factor 2.9 compared to the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 12.9 compared to wild-type enzyme
R68D/K69L/K75V/R76D
-
turnover-number for reaction with NADH and acetolactate is 48fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 3.7 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is lower by a factor 10.8 compared to wild-type enzyme, Km-value for NADH in the reaction with NADPH and acetolactate is 30fold higher compared to wild-type enzyme
R68Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 6.9fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 345 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is 3.4fold higher thahn that of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 18 compared to wild-type enzyme
R76D
-
turnover-number for reaction with NADH and acetolactate is 48fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 4 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is lower by a factor 2.5 compared to wild-type enzyme, Km-value for NADPH in the reaction with NADPH and acetolactate is 55fold higher compared to wild-type enzyme
R76Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 17.1fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 258 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is 5fold higher than that of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 19.5 compared to wild-type enzyme
R76Q/R68A
-
turnover-number for reaction with NADH and acetolactate is 20fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 28 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is comparable to that of wild-type enzyme, Km-value for NADPH in the reaction with NADPH and acetolactate is 22fold higher compared to wild-type enzyme
S414A
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
S414T
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
T84S
G50D/S52D
DELTA1-17
-
mutant with N-terminal 17-residue deletion: cellular localisation similar to wild-type, introduction into an ilv5DELTA strain, lacking the ilv5 gene, complements isoleucine and valine synthesis
DELTA1-33
-
mutant with N-terminal 33-residue deletion: cellular localisation predominatly in the cytosol rather than in mitochondria. Deletion of the N-terminal 33 residues is sufficient to largely impair the protein's targeting to mitochondria. Introduction into an ilv5DELTA strain, lacking the ilv5 gene, complements isoleucine and valine synthesis
DELTA1-40
-
mutant with N-terminal 40-residue deletion: cellular localisation throughout the cytosol rather than in mitochondria
DELTA1-46
-
mutant with N-terminal 46-residue deletion: cellular localisation throughout the cytosol rather than in mitochondria. This mutant shows the largest steady-state protein level. Introduction into an ilv5DELTA strain, lacking the ilv5 gene, does not complements isoleucine and valine synthesis. Introduction into an industrial lager brewing strain, a robust expression of DELTA46 is as effective as that of a wild-type Ilv5p in lowering the total Vicinal diketones production in a 2l scale fermentation trial. Additional expression of DELTA46 does not alter the quality of the resultant beer in terms of contents of aromatic compounds and organic acids
DELTA1-53
-
mutant with N-terminal 53-residue deletion: cellular localisation throughout the cytosol rather than in mitochondria
DELTA1-66
-
mutant with N-terminal 66-residue deletion: weaker cytosolic localisation compared to other mutants. Mutant shows only a small amount of steady-state protein content
DELTA1-83
-
mutant with N-terminal 83-residue deletion: weaker cytosolic localisation compared to other mutants. Mutant shows only a small amount of steady-state protein content
DELTA1-99
-
mutant with N-terminal 99-residue deletion: weaker cytosolic localisation compared to other mutants. Mutant shows only a small amount of steady-state protein content
DELTA423-430/F431S
-
mutant enzyme behaves as an active monomer with reduced thermal stability, KM-value for NADPH does not differ considerably from that for the wild-type enzyme, magnesium affinity is dramatically altered by monomerization
D191G
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
D191K
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
D83G
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
E195A
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
E195K
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
E195S
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
R49A
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
R49E
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
R49G
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53A
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53G
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53K
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53T
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
T84S
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T84S
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
G50D/S52D
mutant engineered for reversal in cofactor specificity for NADH over NADPH
G50D/S52D
-
mutant engineered for reversal in cofactor specificity for NADH over NADPH
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
5 min, about 90% loss of activity at pH 6.2, about 55% loss of activity at pH 6.5, 35% loss of activity oH 7.0, 30% loss of activity at pH 7.5, about 85% loss of activity at pH 8.0, about 90% loss of activity at pH 8.5
95
additional information
-
deletion mutant DELTA423-4301/F431S shows significantly lower temperature stability than wild type enzyme
95
the enzyme is highly thermostable with half-maximal residual activity at 95°C
95
at 95°C, the enzyme is completely unfolded, and it does not refold even when it is slowly cooled to 25°C. Presumably the unfolding process is irreversible, especially after dissociation of the intertwined knot domains
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high activity loss during DEAE-cellulose chromatography, stable towards acetone fractionation and dialysis, unstable towards freezing and thawing
-
unstable in absence of NADPH and Mg2+, very unstable in Tris buffer, 2-mercaptoethanol stabilizes
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°, 20 mM MOPS, 10% glycerol, several months, mutant enzyme DELTA423-431/F431S, no loss of activity
-
-80°, chimeric enzyme composed of Arabidopsis 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, several months, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA-agarose resin column chromatography and Superdex 200 gel filtration
partial
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21
gene ilvC expression in Escherichia coli using an Escherichia coli-Corynebacterium glutamicum shuttle vector pECKA
-
overexpression in Escherichia coli strain BL21(DE3)
the nucleotide sequence coding for the 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 Escherichia coli
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
at 95°C, the enzyme is completely unfolded, and it does not refold even when it is slowly cooled to 25°C. Presumably the unfolding process is irreversible, especially after dissociation of the intertwined knot domains
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
drug development
industry
biofuel production
engineering of Klebsiella pneumoniae to produce 2-butanol from crude glycerol as a sole carbon source by expressing acetolactate synthase (ilvIH), keto-acid reducto-isomerase (ilvC) and dihydroxyacid dehydratase (ilvD) from Klebsiella pneumoniae, and aalpha-ketoisovalerate decarboxylase (kivd) and alcohol dehydrogenase (adhA) from Lactococcus lactis. The engineered strain produces 2-butanol (160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol pathway from the recombinant strain by inactivating alpha-acetolactate decarboxylase (adc) improves the yield of 2-butanol 320 mg/l
biofuel production
-
engineering of Klebsiella pneumoniae to produce 2-butanol from crude glycerol as a sole carbon source by expressing acetolactate synthase (ilvIH), keto-acid reducto-isomerase (ilvC) and dihydroxyacid dehydratase (ilvD) from Klebsiella pneumoniae, and aalpha-ketoisovalerate decarboxylase (kivd) and alcohol dehydrogenase (adhA) from Lactococcus lactis. The engineered strain produces 2-butanol (160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol pathway from the recombinant strain by inactivating alpha-acetolactate decarboxylase (adc) improves the yield of 2-butanol 320 mg/l
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drug development
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the enzyme is a target for herbicide drug development, computer-aided drug design
drug development
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the enzyme is a promising target for the design of herbicides
drug development
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the enzyme is a promising target for the design of herbicides
industry
Sac-KARI is one of the rare enzymes that displays high activity at elevated temperatures, a broad range of pH tolerance and is able to utilize both NADH and NADPH as cofactors. These properties make it a potential candidate for use in metabolic engineering or industrial applications under anaerobic or harsh conditions
industry
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Sac-KARI is one of the rare enzymes that displays high activity at elevated temperatures, a broad range of pH tolerance and is able to utilize both NADH and NADPH as cofactors. These properties make it a potential candidate for use in metabolic engineering or industrial applications under anaerobic or harsh conditions
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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brenda
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58
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Spinacia oleracea
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Wang, B.; Li, Z.; Li, Y.; Wang, S.
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24
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Oryza sativa
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389
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Oryza sativa (Q65XK0), Oryza sativa
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Oryza sativa
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4
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Oryza sativa, Brassica rapa subsp. oleifera, Echinochloa crus-galli
-
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424
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Escherichia coli (P05793), Escherichia coli
brenda
Cahn, J.K.; Brinkmann-Chen, S.; Spatzal, T.; Wiig, J.A.; Buller, A.R.; Einsle, O.; Hu, Y.; Ribbe, M.W.; Arnold, F.H.
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brenda
Oh, B.R.; Heo, S.Y.; Lee, S.M.; Hong, W.K.; Park, J.M.; Jung, Y.R.; Kim, D.H.; Sohn, J.H.; Seo, J.W.; Kim, C.H.
Production of 2-butanol from crude glycerol by a genetically-engineered Klebsiella pneumoniae strain
Biotechnol. Lett.
36
57-62
2014
Klebsiella pneumoniae subsp. pneumoniae (A6TGG1), Klebsiella pneumoniae subsp. pneumoniae ATCC 700721 (A6TGG1)
brenda
Reisse, S.; Garbe, D.; Brueck, T.
Identification and optimization of a novel thermo- and solvent stable ketol-acid reductoisomerase for cell free isobutanol biosynthesis
Biochimie
108
76-84
2015
Meiothermus ruber (D3PT81), Meiothermus ruber, Meiothermus ruber DSM 1279 (D3PT81)
brenda
Tadrowski, S.; Pedroso, M.M.; Sieber, V.; Larrabee, J.A.; Guddat, L.W.; Schenk, G.
Metal ions play an essential catalytic role in the mechanism of ketol-acid reductoisomerase
Chemistry
22
7427-7436
2016
Oryza sativa, Escherichia coli
brenda
Lv, Y.; Kandale, A.; Wun, S.J.; McGeary, R.P.; Williams, S.J.; Kobe, B.; Sieber, V.; Schembri, M.A.; Schenk, G.; Guddat, L.W.
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283
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Mycobacterium tuberculosis (P9WKJ7), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WKJ7)
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Verdel-Aranda, K.; Lopez-Cortina, S.T.; Hodgson, D.A.; Barona-Gomez, F.
Molecular annotation of ketol-acid reductoisomerases from Streptomyces reveals a novel amino acid biosynthesis interlock mediated by enzyme promiscuity
Microb. Biotechnol.
8
239-252
2015
Corynebacterium glutamicum, Escherichia coli, Streptomyces ambofaciens (A0A0K2AZ61), Streptomyces ambofaciens ATCC 23877 (A0A0K2AZ61), Streptomyces avermitilis (Q59818), Streptomyces avermitilis DSM 46492 (Q59818), Streptomyces coelicolor (Q9Z565), Streptomyces coelicolor (Q9FBT8), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9Z565), Streptomyces coelicolor BAA-471 (Q9FBT8), Streptomyces griseus, Streptomyces lividans (D6ERQ9), Streptomyces lividans (D6EC76), Streptomyces lividans, Streptomyces lividans TK24 (D6ERQ9), Streptomyces lividans TK24 (D6EC76), Streptomyces pristinaespiralis, Streptomyces viridifaciens
brenda
Brinkmann-Chen, S.; Flock, T.; Cahn, J.; Snow, C.; Brustad, E.; McIntosh, J.; Meinhold, P.; Zhang, L.; Arnold, F.
General approach to reversing ketol-acid reductoisomerase cofactor dependence from NADPH to NADH
Proc. Natl. Acad. Sci. USA
110
10946-10951
2013
Alicyclobacillus acidocaldarius subsp. acidocaldarius (C8WR67), Methanococcus aeolicus (A6UW80), Methanococcus aeolicus DSM 17508 (A6UW80)
brenda
Wun, S.J.; Johnson, L.A.; You, L.; McGeary, R.P.; Brueck, T.; Schenk, G.; Guddat, L.W.
Inhibition studies of ketol-acid reductoisomerases from pathogenic microorganisms
Arch. Biochem. Biophys.
692
108516
2020
Mycobacterium tuberculosis (P9WKJ7), Mycobacterium tuberculosis, Campylobacter jejuni, Mycobacterium tuberculosis ATCC 25618 (P9WKJ7)
brenda
Wang, B.L.; Zhang, L.Y.; Liu, X.H.; Ma, Y.; Zhang, Y.; Li, Z.M.; Zhang, X.
Synthesis, biological activities and SAR studies of new 3-substitutedphenyl-4-substituted benzylideneamino-1,2,4-triazole Mannich bases and bis-Mannich bases as ketol-acid reductoisomerase inhibitors
Bioorg. Med. Chem. Lett.
27
5457-5462
2017
Oryza sativa Japonica Group (Q65XK0)
brenda
Yu, M.J.; Wu, J.; Chen, S.L.
Mechanism and inhibitor exploration with binuclear Mg ketol-acid reductoisomerase targeting the biosynthetic pathway of branched-chain amino acids
ChemBioChem
21
381-391
2020
Staphylococcus aureus (Q2FWK4), Staphylococcus aureus NCTC 8325 (Q2FWK4)
brenda
Patel, K.M.; Teran, D.; Zheng, S.; Kandale, A.; Garcia, M.; Lv, Y.; Schembri, M.A.; McGeary, R.P.; Schenk, G.; Guddat, L.W.
Crystal structures of Staphylococcus aureus ketol-acid reductoisomerase in complex with two transition state analogues that have biocidal activity
Chemistry
23
18289-18295
2017
Staphylococcus aureus (Q2FWK4), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FWK4)
brenda
Bayaraa, T.; Kurz, J.L.; Patel, K.M.; Hussein, W.M.; Bilyj, J.K.; West, N.P.; Schenk, G.; McGeary, R.P.; Guddat, L.W.
Discovery, synthesis and evaluation of a ketol-acid reductoisomerase inhibitor
Chemistry
26
8958-8968
2020
Mycobacterium tuberculosis (P9WKJ7), Mycobacterium tuberculosis, Staphylococcus aureus (Q2FWK4), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FWK4)
brenda
Lin, X.; Kurz, J.L.; Patel, K.M.; Wun, S.J.; Hussein, W.M.; Lonhienne, T.; West, N.P.; McGeary, R.P.; Schenk, G.; Guddat, L.W.
Discovery of a pyrimidinedione derivative with potent inhibitory activity against Mycobacterium tuberculosis ketol-acid reductoisomerase
Chemistry
27
3130-3141
2021
Mycobacterium tuberculosis (P9WKJ7), Mycobacterium tuberculosis (A5U713), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKJ7)
brenda
Kim, G.; Shin, D.; Lee, S.; Yun, J.; Lee, S.
Crystal structure of ILvC, a ketol-acid reductoisomerase, from Streptococcus pneumoniae
Crystals
9
551
2019
Streptococcus pneumoniae (Q04M32)
-
brenda
Krishna, V.S.; Zheng, S.; Rekha, E.M.; Nallangi, R.; Sai Prasad, D.V.; George, S.E.; Guddat, L.W.; Sriram, D.
Design and development of ((4-methoxyphenyl)carbamoyl) (5-(5-nitrothiophen-2-yl)-1,3,4-thiadiazol-2-yl)amide analogues as Mycobacterium tuberculosis ketol-acid reductoisomerase inhibitors
Eur. J. Med. Chem.
193
112178
2020
Mycobacterium tuberculosis (P9WKJ7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKJ7)
brenda
Lee, D.; Hong, J.; Kim, K.J.
Crystal structure and biochemical characterization of ketol-acid reductoisomerase from Corynebacterium glutamicum
J. Agric. Food Chem.
67
8527-8535
2019
Corynebacterium glutamicum (Q57179), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q57179)
brenda
Chen, C.Y.; Chang, Y.C.; Lin, B.L.; Lin, K.F.; Huang, C.H.; Hsieh, D.L.; Ko, T.P.; Tsai, M.D.
Use of cryo-EM To uncover structural bases of pH effect and cofactor bispecificity of ketol-acid reductoisomerase
J. Am. Chem. Soc.
141
6136-6140
2019
Saccharolobus solfataricus
brenda
Krishna, V.S.; Zheng, S.; Rekha, E.M.; Guddat, L.W.; Sriram, D.
Discovery and evaluation of novel Mycobacterium tuberculosis ketol-acid reductoisomerase inhibitors as therapeutic drug leads
J. Comput. Aided Mol. Des.
33
357-366
2019
Mycobacterium tuberculosis (P9WKJ7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKJ7)
brenda
Chen, C.; Ko, T.; Lin, K.; Lin, B.; Huang, C.; Chiang, C.; Horng, J.
NADH/NADPH bi-cofactor-utilizing and thermoactive ketol-acid reductoisomerase from Sulfolobus acidocaldarius
Sci. Rep.
8
7176
2018
Sulfolobus acidocaldarius (Q4J8K9), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius ATCC 33909 (Q4J8K9)
brenda
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