Information on EC 1.1.1.86 - ketol-acid reductoisomerase (NADP+)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.1.86
-
RECOMMENDED NAME
GeneOntology No.
ketol-acid reductoisomerase (NADP+)
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
-
-
-
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
bifunctional enzyme that catalyses two different reactions at a common active site, an isomerization consisting of an alkyl migration, followed by an NADPH-dependent reduction of a-ketoacid
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
active site structure
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
catalytic mechanism, overview
-
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
active site structure and catalytic mechanism, mechanism of induced fit, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
rearrangement
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-isoleucine biosynthesis I (from threonine)
-
-
L-isoleucine biosynthesis III
-
-
L-valine biosynthesis
-
-
pyruvate fermentation to isobutanol (engineered)
-
-
isoleucine metabolism
-
-
valine metabolism
-
-
Valine, leucine and isoleucine biosynthesis
-
-
Pantothenate and CoA biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
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)+]).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-hydroxy-3-keto acid reductoisomerase
-
-
-
-
acetohydroxy acid isomeroreductase
-
-
-
-
acetohydroxy acid isomeroreductase
-
-
acetohydroxy acid isomeroreductase
-
-
acetohydroxy acid isomeroreductase
-
-
acetohydroxy acid reductoisomerase
-
-
-
-
acetohydroxy-acid isomeroreductase
-
-
-
-
acetohydroxy-acid reductoisomerase
-
-
-
-
acetolactate reductoisomerase
-
-
-
-
alpha-keto-beta-hydroxylacil reductoisomerase
-
-
-
-
alpha-keto-beta-hydroxylacyl reductoisomerase
-
-
-
-
class II ketol-acid reductoisomerase
-
-
dehydrogenase, dihydroxyisovalerate (isomerizing)
-
-
-
-
dihydroxyisovalerate dehydrogenase (isomerizing)
-
-
-
-
isomerase, ketol acid reducto-
-
-
-
-
isomeroreductase
-
-
-
-
KARI
-
-
-
-
ketol-acid reductoisomerase
-
-
ketol-acid reductoisomerase
-
-
ketol-acid reductoisomerase
-
-
ketol-acid reductoisomerase
-
-
reductoisomerase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9075-02-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a histatin-resistant derivative of Candida albicans strain 132A is used
-
-
Manually annotated by BRENDA team
strain ATCC 13032, gene ilvC
-
-
Manually annotated by BRENDA team
Digitaria adscendens
-
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
morning glory
-
-
Manually annotated by BRENDA team
gene Pi-kari1
-
-
Manually annotated by BRENDA team
black nightshade
-
-
Manually annotated by BRENDA team
overexpressed in Escherichia coli
-
-
Manually annotated by BRENDA team
spinach, multiple enzyme forms: iso 1, 2 and 3
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 pathway
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH
show the reaction diagram
-
the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview
-
?
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
-
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
-
conformational changes in a plant ketol-acid reductoisomerase upon Mg2+ and NADPH binding, overview
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
-
the enzyme performs a two-step reaction of an alkyl migration followed by an NADPH-dependent reduction rection
-
r
2-aceto-2-hydroxybutyrate + NADP+
(2R,3R)-2,3-dihydroxy-3-methylvalerate + NADPH + H+
show the reaction diagram
-
-
-
r
2-aceto-2-hydroxybutyrate + NADPH
2,3-dihydroxy-3-methylvalerate + NADP+
show the reaction diagram
-
the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview
-
?
2-acetolactate + NADP+
(2R)-2,3-dihydroxy-3-isovalerate + NADPH + H+
show the reaction diagram
-
-
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
-
-
?
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
not reversible at pH 7.5, reversible at pH 9-10, enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of valine synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
second common reaction in the biosynthesis of the branched chain amino acids
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+ + H+
show the reaction diagram
-
the enzyme is the second of the valine pathway
-
r
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
show the reaction diagram
-
-
-
?
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
show the reaction diagram
-
-
?
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
show the reaction diagram
-
the enzyme is involved in biosynthesis of the branched chain amino acid isoleucine, pathway overview
-
?
2-acetolactate + NADPH + H+
3-hydroxy-2-ketobutyrate + NADP+
show the reaction diagram
-
-
-
r
2-ketobutyrate + NADPH + H+
?
show the reaction diagram
-
-
-
-
r
2-ketoisovalerate + NADPH + H+
?
show the reaction diagram
-
-
-
-
r
2-ketopantoate + NADPH + H+
?
show the reaction diagram
-
-
-
-
r
2-ketovalerate + NADPH + H+
?
show the reaction diagram
-
-
-
-
r
3-hydroxy-3-methyl-2-ketobutyrate + NADP+
?
show the reaction diagram
-
-
-
-
r
3-hydroxypyruvate + NADPH + H+
?
show the reaction diagram
-
-
-
-
r
acetolactate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
show the reaction diagram
-
-
-
r
acetolactate + NADPH + H+
2,3-dihydroxy-2-methylbutanoate + NADP+
show the reaction diagram
-
-
-
r
NADP+ + 3-hydroxy-3-methyl-2-oxobutanoate
NADPH + acetolactate
show the reaction diagram
-
-
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
-
-
-
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
-
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
-
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
-
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
-
-
-
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
-
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
-
-
?
NADPH + 2-aceto-2-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
activity is 6-10times greater than that for 2-acetolactate
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
-
-
?
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
not reversible at pH 7.5, reversible at pH 9-10
-
?, r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
alpha-keto-beta-hydroxyisovalerate is not a free intermediate
-
?, r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
show the reaction diagram
-
ordered reaction with NADPH and the acetohydroxy acid adding in that order, and dihydroxy acid released before NADP+. 4 mol of NADPH bind per mol of enzyme
-
?
NADPH + 2-oxo-3-hydroxyisovalerate
NADP+ + alpha,beta-dihydroxyisovalerate
show the reaction diagram
-
-
-
?
NADPH + alpha-aceto-alpha-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
enzyme of isoleucine biosynthesis
-
?
pyruvate + NADPH + H+
?
show the reaction diagram
-
-
-
-
r
hydroxypyruvate + NADPH
glycerate + NADP+
show the reaction diagram
-
-
?
additional information
?
-
-
the enzyme catalyzes the isomerization of 2-oxo-3-hydroxyisovalerate to 2-acetolactate
-
-
-
additional information
?
-
-
the enzyme catalyses the second reaction in the biosynthesis of the branched-chain amino acids
-
-
-
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
-
-
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
-
-
additional information
?
-
-
enzyme expression is up-regulated in germinating cysts developing appressoria, which are important for interaction of pathogen and host plants tomato and potato
-
-
-
additional information
?
-
-
the enzyme is involved in biosynthesis of branched amino acids valine, isoleucine, and leucine, pathway overview
-
-
-
additional information
?
-
-
the enzyme is involved in biosynthesis of branched chain amino acids valine, isoleucine, and leucine, effects of KARI inhibition effects on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
-
-
-
additional information
?
-
-
structure-biological activity relationship, overview
-
-
-
additional information
?
-
-
KARI catalyzes two reactions: alkyl migration and reduction. Structure-function relationship, effects of ligand binding, MG2+ and NADPH, on the enzyme conformation, overview
-
-
-
additional information
?
-
-
structure-activity relationship
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
-
-
-
r
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+
(S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
show the reaction diagram
-
-
-
r
2-aceto-2-hydroxybutyrate + NADPH
2,3-dihydroxy-3-methylvalerate + NADP+
show the reaction diagram
-
-
-
?
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
not reversible at pH 7.5, reversible at pH 9-10, enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
Q01292
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
enzyme of valine synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
second common reaction in the biosynthesis of the branched chain amino acids
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+ + H+
show the reaction diagram
-
the enzyme is the second of the valine pathway
-
r
NADPH + alpha-aceto-alpha-hydroxybutyrate
NADP+ + ?
show the reaction diagram
-
enzyme of isoleucine biosynthesis
-
?
2-acetolactate + NADPH
2,3-dihydroxyisovalerate + NADP+
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme catalyses the second reaction in the biosynthesis of the branched-chain amino acids
-
-
-
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
-
-
additional information
?
-
-
the enzyme is involved in the biosynthesis of the branched-chain amino acids
-
-
-
additional information
?
-
-
enzyme expression is up-regulated in germinating cysts developing appressoria, which are important for interaction of pathogen and host plants tomato and potato
-
-
-
additional information
?
-
-
the enzyme is involved in biosynthesis of branched amino acids valine, isoleucine, and leucine, pathway overview
-
-
-
additional information
?
-
-
the enzyme is involved in biosynthesis of branched chain amino acids valine, isoleucine, and leucine, effects of KARI inhibition effects on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
-
-
-
additional information
?
-
-
structure-biological activity relationship, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
4 mol of NADPH bind per mol of enzyme
NADPH
-
required, the majority of the NADP+ molecule binds to the N-domain of KARI with polar contacts with 11 residues, including W133, G134, S135, Q136, R162, S165, S167, S201, D202, Q205, and G254. There are also contacts with the C-domain, although these are much fewer and involve only the phosphoryl oxygen atoms and the oxygen and nitrogen atoms of the nicotinamide group in NADPH, forming contacts with C517, S518, and T519, and with R589 in the polypeptide
NADPH
binding of NADPH is enthalpy driven. NADPH binding may have an opposing effect to that of Mg2+ binding by inducing an increase in structural stability
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
the reaction requires a divalent metal ion
Mg2+
-
optimum concentration 5 mM; required
Mg2+
-
Km: 0.42 mM; required; with acetolactate as substrate , Mg2+ is the only divalent metal ion that supports enzyme catalysis
Mg2+
-
Km: 0.35 mM, pH 10, reaction with acetolactate; Km: 0.45 mM, pH 6.7, reaction with acetolactate; Km: 0.4 mM, pH 8.5; required
Mg2+
-
Km for Mg2+: 0.0045 mM, at pH 8.2, 30C; required
Mg2+
-
required
Mg2+
-
Km: 0.5 mM; required
Mg2+
-
required; two ions bind to enzyme
Mg2+
-
the reaction requires a divalent metal ion
Mg2+
-
required
Mg2+
-
required, KM: 0.00324 mM
Mg2+
-
-
Mg2+
-
required for the alkyl migration reaction step
Mg2+
-
required for the alkyl migration reaction, Km is 0.0072 mM, binding structure, overview
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
Mn2+
-
activates reaction with 3-hydroxy-3-methyl-2-oxobutanoate, no effect on reaction with acetolactate
Mn2+
-
the reaction requires a divalent metal ion
additional information
-
no metal ions required
additional information
-
metal ions other than Mg2+ are inhibitory
additional information
-
Mn2+, Co2+, Ni2+, Zn2+, Ca2+, Cu2+ and Co3+ can not substitute for Mg2+
additional information
-
no metal ions required
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1-cyclopropanedicarboxylic acid
-
i.e. CPCA, inhibition in vivo, effect on pea root length, shoot length, and fermentative metabolism, effects of KARI inhibition effects on other enzymes, such as alcohol dehydrogenase, EC 1.1.1.1, pyruvate dehydrogenase, EC 4.1.1.1, lactate dehydrogenase, EC 1.1.1.27, and alanine aminotransferase, EC 2.6.1.2, overview
1-aminocarbonyl-cyclopropane carboxylate
-
-
1-aminocarbonylcyclopropanecarboxylate
-
-
1-carbamoylcyclopropanecarboxylic acid
-
-
1-cyano-cyclopropane carboxylate
-
-
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-(2-methylphenyl)cyclopropanecarboxamide
-
inhibition rate: 100%
1-cyano-N-(4-methoxyphenyl)cyclopropanecarboxamide
-
inhibition rate: 3.95%
1-cyano-N-(4-methylphenyl)cyclopropanecarboxamide
-
inhibition rate: 61.21%
1-cyano-N-phenylcyclopropanecarboxamide
-
inhibition rate: 77.23%
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%
1-cyanocyclopropanecarboxylate
-
-
1-cyanocyclopropanecarboxylic acid
-
inhibition rate: 100%
1-cyanocyclopropanecarboxylic acid
-
-
1-hydroxycyclopropanecarboxylate
-
-
11-dihydro-5H-dibenzo[b,e][1,4]diazepin-11-one
-
-
2,3-dihydroxy-3-isovalerate
-
-
2,3-dihydroxy-3-methylbutanoic acid
-
linear noncompetitive inhibitor of both 2-acetolactate and NADPH
2,3-dihydroxy-3-methylbutyrate
-
-
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-(4-benzylpiperazin-1-yl)-N-arylacetamide
-
-
2-(4-methoxybenzamido)benzoic acid
-
-
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
-
; competitive, reversible
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-hydroxy-2-methyl-3-oxopentanoate
-
-
2-Hydroxy-2-methylbutyrate
-
0.01 M 45% inhibition
2-Hydroxybutyrate
-
0.01 M, 48% inhibition
2-Hydroxyisovalerate
-
0.01 M, 38% inhibition
2-Hydroxyisovalerate
-
noncompetitive
2-Methyllactate
-
0.001 M, 61% inhibition; competitive
2-Methyllactate
-
uncompetitive; uncompetitive with respect to NADPH
2-Methyllactate
-
competitive
2-Oxo-3-hydroxyisovalerate
-
0.001 mM, 58% inhibition
2-oxoisovalerate
-
0.01 M, 21% inhibition
2-[2-(4-morpholino)]acetamido-4-methylthiazole
-
-
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
3-aminopyridine-NADP+
-
-
3-hydroxy-3-methyl-2-oxobutanoic acid
-
-
4,4'-(pentamethylenedioxy)dibenzamidne bis(2-hydroxyethanesulfonate)
-
binding structure and inhibition mechanism, overview
4-(2,4-dichlorophenoxy)benzenecarboximidamide
-
-
4-(2-fluorophenoxy)benzenecarboximidamide
-
-
4-(3-chlorophenoxy)benzenecarboximidamide
-
-
4-(4-chlorophenoxy)benzenecarboximidamide
-
-
4-phenoxybenzenecarboximidamide
-
-
arsenite
-
slight inhibition
ascorbic acid
-
slight inhibition with 2-acetolactate as substrate
cyclopropane-1,1-dicarboxylate
-
a competitive slow-, tight-binding inhibitor
cyclopropane-1,1-dicarboxylate
-
-
cyclopropane-1,1-dicarboxylic acid
-
-
dimethylmalonate
-
slow-binding inhibitor
ethyl 1-cyanocyclopropanecarboxylate
-
inhibition rate: 0%
ethyl 3-hydroxy-2-oxobutanoate
-
-
ethyl 3-methyl-3-hydroxy-2-oxobutanoate
-
-
ethyl [(2-chlorophenyl)(hydroxy)amino](oxo)acetate
-
-
ethyl [hydroxy(2-methylphenyl)amino](oxo)acetate
-
-
ethyl [hydroxy(4-methylphenyl)amino](oxo)acetate
-
-
ethyl [[4-(cyanomethyl)phenyl](hydroxy)amino](oxo)acetate
-
-
ethylene glycol
-
exhibits competitive and uncompetitive inhibition
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
L-ascorbic acid
-
slightly inhibitory with alpha-acetolactate as substrate
methyl [hydroxy(1-methylethyl)amino](oxo)acetate
-
-
N'-(5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-(2-methyl-phenyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-(3-methyl-phenyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
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'-(5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-(4-nitrophenyl)-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-butyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-ethyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-furan-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-heptyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-iso-propyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-isopropyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-methyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
-
N'-(5-octyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-pentyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-phenyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N'-(5-propyl-1,3,4-thiadiazol-2-yl)-N-cyclopropyformyl-thiourea
-
-
N-(2-(piperidin-1-yl)ethyl)phthalimide
-
-
N-(3-bromophenyl)-1-cyanocyclopropanecarboxamide
-
inhibition rate: 17.25%
N-(3-chlorophenyl)-1-cyanocyclopropanecarboxamide
-
inhibition rate: 0%
N-(4-bromophenyl)-1-cyanocyclopropanecarboxamide
-
inhibition rate: 32.23%
N-(4-chlorophenyl)-1-cyanocyclopropanecarboxamide
-
inhibition rate: 93.92%
N-(5-substituted-1,3,4-thiadiazol-2-yl)-N-cyclopropylformyl-thiourea
-
-
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
-
competitive
N-Hydroxy-N-isopropyloxamate
-
-
N-Hydroxy-N-isopropyloxamate
-
i.e. IpOHA, potent competitive inhibitor in vitro but weak in vivo
N-Hydroxy-N-isopropyloxamate
-
i.e. IpOHA, potent competitive inhibitor in vitro but weak in vivo
N-Hydroxy-N-isopropyloxamate
-
-
NADP+
-
linear non-competitive with respect to 2-acetolactate, linear competitive inhibitor of NADPH
NADP+
-
competitive with NADPH
NADP+
-
product inhibition
Mn2+
-
with acetolactate as substrate, Mn2+ behaves as a competitive inhibitor in presence of Mg2+
additional information
-
no inhibition with p-mercuribenzoate, cysteine, 2-mercaptoethanol
-
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
-
computer-aided drug design, overview
-
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 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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
5 mM, enhances activity 2-hydroxy-2-ethyl-3-oxobutanoate as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
2-aceto-2-hydroxybutanoate
-
pH 8.2, 30C, 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
0.002
2-aceto-2-hydroxybutyrate
-
pH 7.4, 25C
0.01
2-aceto-2-hydroxybutyrate
-
pH 8.2, 30C
0.037
2-aceto-2-hydroxybutyrate
-
pH 8, 30C, isoenzyme 1
0.038
2-aceto-2-hydroxybutyrate
-
pH 7.5, 25C
0.12
2-aceto-2-hydroxybutyrate
-
-
0.16
2-aceto-2-hydroxybutyrate
-
pH 7.5, 25C
0.01
2-acetolactate
-
pH 8.2, 30C
0.011
2-acetolactate
-
pH 7.5, 25C
0.014
2-acetolactate
-
pH 7.4, 25C
0.025
2-acetolactate
-
pH 8, 30C, isoenzyme 1
0.042
2-acetolactate
-
pH 8.0, 30C, recombinant enzyme
0.25
2-acetolactate
-
pH 8.0, 37C, wild-type enzyme
0.29
2-acetolactate
-
30C, with 2-acetolactate or 2-aceto-2-hydroxybutyrate as substrate
0.32
2-acetolactate
-
pH 7.5, 25C
0.356
2-acetolactate
-
pH 8.0, 37C, mutant E221D
0.414
2-acetolactate
-
pH 8.0, 37C, mutant S414T
0.711
2-acetolactate
-
pH 8.0, 37C, mutant S414A
0.922
2-acetolactate
-
pH 8.0, 37C, mutant H213D
0.929
2-acetolactate
-
pH 8.0, 37C, mutant H132Q
1.218
2-acetolactate
-
pH 8.0, 37C, mutant H155R
1.4
2-acetolactate
-
pH 7.3, 30C
2.028
2-acetolactate
-
pH 8.0, 37C, mutant E289D
5.5
2-acetolactate
-
-
4.56
2-Ketobutyrate
-
pH 8.0, 37C, wild-type enzyme
6.91
2-ketoisovalerate
-
pH 8.0, 37C, wild-type enzyme
0.17
2-ketopantoate
-
pH 8.0, 37C, wild-type enzyme
3.15
2-Ketovalerate
-
pH 8.0, 37C, wild-type enzyme
0.21
3-hydroxy-2-ketobutyrate
-
pH 8.0, 37C, wild-type enzyme
0.27
3-hydroxy-3-methyl-2-ketobutyrate
-
pH 8.0, 37C, wild-type enzyme
0.334
3-hydroxypyruvate
-
pH 8.0, 37C, mutant S414A
0.441
3-hydroxypyruvate
-
pH 8.0, 37C, mutant E213Q
0.588
3-hydroxypyruvate
-
pH 8.0, 37C, mutant E393Q
0.818
3-hydroxypyruvate
-
pH 8.0, 37C, mutant H132K
1.101
3-hydroxypyruvate
-
pH 8.0, 37C, mutant S414T
1.37
3-hydroxypyruvate
-
pH 8.0, 37C, mutant E221D
2.66
3-hydroxypyruvate
-
pH 8.0, 37C, mutant K155E
2.96
3-hydroxypyruvate
-
pH 8.0, 37C, wild-type enzyme
3.32
3-hydroxypyruvate
-
pH 8.0, 37C, mutant E393D
3.67
3-hydroxypyruvate
-
pH 8.0, 37C, mutant E213D
7.43
3-hydroxypyruvate
-
pH 8.0, 37C, mutant H132Q
7.64
3-hydroxypyruvate
-
pH 8.0, 37C, mutant D217N
8.5
3-hydroxypyruvate
-
pH 8.0, 37C, mutant E389D
8.88
3-hydroxypyruvate
-
pH 8.0, 37C, mutant E389Q
13.6
3-hydroxypyruvate
-
pH 8.0, 37C, mutant K155R
15.3
3-hydroxypyruvate
-
pH 8.0, 37C, mutant K155Q
0.893
Hydroxypyruvate
-
pH 8.0, 30C, recombinant enzyme
0.019
NADH
-
pH 8.0, 22C, mutant enzyme R68D/K69L/K75V/R76D
0.082
NADH
-
pH 8, 22C, mutant enzyme R76D
0.101
NADH
-
pH 8.2, 30C
0.193
NADH
-
pH 8, 22C, mutant enzyme R76Q/R68A
0.207
NADH
-
pH 8.0, 22C, wild type enzyme
0.0089
NADP+
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K69L
0.0112
NADP+
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K75Q
0.029
NADP+
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R68Q
0.072
NADP+
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R76Q
0.00016
NADPH
-
pH 8.0, 37C, mutant E213D
0.0017
NADPH
-
pH 8.2, 30C
0.002
NADPH
-
pH 7.4, 25C
0.0025
NADPH
-
pH 8.0, 22C, reaction with acetolactate, mutant enzyme K75Q
0.00253
NADPH
-
pH 8.0, 37C, wild-type enzyme
0.0031
NADPH
-
pH 8.0, 37C, mutant H132K
0.0035
NADPH
-
pH 8.2, 30C, wild type enzyme
0.0043
NADPH
-
pH 7.5, 25C
0.0048
NADPH
-
pH 8.0, 37C, mutant E393D
0.005
NADPH
-
pH 8.0, 37C, mutant D217N; pH 8.0, 37C, mutant S414T
0.0052
NADPH
-
pH 8.2, 30C, deletion mutant DELTA423-430/F431S
0.0057
NADPH
-
pH 8, 30C, isoenzyme 1
0.007
NADPH
-
pH 8.0, 22C, wild type enzyme
0.007
NADPH
-
pH 8.2, 30C, 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
0.0072
NADPH
-
pH 8.0, 30C, recombinant enzyme
0.0073
NADPH
-
pH 8.0, 37C, mutant K155R
0.0076
NADPH
-
pH 8.0, 22C, reaction with acetolactate, mutant enzyme K69L
0.00804
NADPH
-
pH 8.0, 37C, mutant K155E
0.0084
NADPH
-
pH 8.0, 37C, mutant S414A
0.0093
NADPH
-
pH 8.0, 37C, mutant K155Q
0.015
NADPH
-
30C with 2-acetolactate or 2-aceto-2-hydroxybutyrate as substrate
0.02
NADPH
-
pH 8.0, 37C, mutant E221D; pH 8.0, 37C, mutant E221Q
0.023
NADPH
-
pH 8.0, 37C, mutant E389D
0.0245
NADPH
-
pH 8.0, 22C, reaction with 2-acetolactate, mutant enzyme R68QL
0.0365
NADPH
-
pH 8.0, 22C, reaction with 2-acetolactate, mutant enzyme R76Q
0.069
NADPH
-
pH 8.0, 37C, mutant H132Q
0.08
NADPH
-
pH 8.0, 37C, mutant D217E
0.16
NADPH
-
pH 8, 22C, mutant enzyme R76Q/R68A
0.222
NADPH
-
pH 8, 22C, mutant enzyme R68D/K69L/K75V/R76D
0.401
NADPH
-
pH 8, 22C, mutant enzyme R76D
11.2
NADPH
-
pH 7.3, 30C
1.54
pyruvate
-
pH 8.0, 37C, wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00417
2,3-Dihydroxy-3-methylbutanoate
Escherichia coli
-
pH 7.4, 25C
78.3
2-aceto-2-hydroxybutyrate
Salmonella enterica subsp. enterica serovar Typhimurium
-
30C
1.8
2-acetolactate
Escherichia coli
-
pH 7.4, 25C
2.231
2-acetolactate
Escherichia coli
-
pH 8.0, 37C
18.3
2-acetolactate
Salmonella enterica subsp. enterica serovar Typhimurium
-
30C
0.167
2-Ketobutyrate
Escherichia coli
-
pH 8.0, 37C
0.182
2-ketoisovalerate
Escherichia coli
-
pH 8.0, 37C
0.194
2-ketopantoate
Escherichia coli
-
pH 8.0, 37C
0.05
2-Ketovalerate
Escherichia coli
-
pH 8.0, 37C
0.594
3-hydroxy-2-ketobutyrate
Escherichia coli
-
pH 8.0, 37C
3.511
3-hydroxy-3-methyl-2-ketobutyrate
Escherichia coli
-
pH 8.0, 37C
5.376
3-hydroxypyruvate
Escherichia coli
-
pH 8.0, 37C
0.00183
NADH
Escherichia coli
-
wild type enzyme
0.0367
NADH
Escherichia coli
-
pH 8, 22C, mutant enzyme R76Q/R68A
0.0883
NADH
Escherichia coli
-
pH 8, 22C, mutant enzyme R68D/K69L/K75V/R76D and mutant enzyme R76D
0.00015
NADP+
Escherichia coli
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R68Q
0.0002
NADP+
Escherichia coli
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R76Q
0.000317
NADP+
Escherichia coli
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K69L
0.000667
NADP+
Escherichia coli
-
pH 8.0, 22C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K75Q
0.0000933
NADPH
Escherichia coli
-
pH 8.0, 22C, reaction with acetolactate, mutant enzyme K75Q
0.00433
NADPH
Escherichia coli
-
pH 8, 22C, mutant enzyme R76Q/R68A
0.00617
NADPH
Escherichia coli
-
pH 8.0, 22C, reaction with acetolactate, mutant enzyme R76Q
0.00667
NADPH
Escherichia coli
-
pH 8.0, 22C, reaction with acetolactate, mutant enzyme R68Q
0.03
NADPH
Escherichia coli
-
pH 8, 22C, mutant enzyme R76D
0.0328
NADPH
Escherichia coli
-
pH 8.0, 22C, mutant enzyme R68D/K69L/K75V/R76D
0.12
NADPH
Escherichia coli
-
pH 8, 22C, wild type enzyme
0.212
NADPH
Escherichia coli
-
pH 8.0, 22C, reaction with acetolactate, mutant enzyme K69L
0.021
pyruvate
Escherichia coli
-
pH 8.0, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
1-aminocarbonyl-cyclopropane carboxylate
-
-
0.0203
1-aminocarbonylcyclopropanecarboxylate
-
pH 8.0, 30C, recombinant enzyme
0.031
1-carbamoylcyclopropanecarboxylic acid
-
pH 8.0, 30C
207.9
1-cyano-N-[[(E)-(3,3-dichloroprop-1-yn-1-yl)diazenyl]sulfanyl]cyclopropanecarboxamide
-
-
0.0585
1-cyanocyclopropanecarboxylate
-
pH 8.0, 30C, recombinant enzyme
0.095
1-cyanocyclopropanecarboxylic acid
-
pH 8.0, 30C
95.3
1-cyanocyclopropanecarboxylic acid
-
-
0.0056
1-hydroxycyclopropanecarboxylate
-
pH 8.0, 30C, recombinant enzyme
0.145
2,3-dihydroxy-3-isovalerate
-
pH 8.2, 30C, (2S)-2-aceto-2-hydroxybutanoate as variable substrate, 0.250 mM NADPH as fixed substrate
0.095
2,3-dihydroxyisovalerate
-
pH 8.2, 30C, (2S)-2-acetolactate as variable substrate, 0.250 mM NADPH as fixed substrate
0.935
2,3-dihydroxyisovalerate
-
pH 8.2, 30C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate
1.5
2,3-dihydroxyisovalerate
-
pH 8.2, 30C, 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, 25C, with 2-aceto-2-hydroxybutyrate as substrate
0.00046
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
pH 7.5, 25C, with 2-acetolactate as substrate
0.24
2-hydroxy-2-methyl-3-oxopentanoate
-
pH 8.2, 30C, (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, 30C, (2S)-2-acetolactate as variable substrate, 0.075 mM NADPH as fixed substrate
1.7
2-hydroxy-2-methyl-3-oxopentanoate
-
pH 8.2, 30C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate
3.6
2-hydroxy-2-methyl-3-oxopentanoate
-
pH 8.2, 30C, NADPH as variable substrate, 0.2 mM (2S)-2-aceto-2-hydroxybutanoate as fixed substrate
0.35
4,4'-(pentamethylenedioxy)dibenzamidne bis(2-hydroxyethanesulfonate)
-
-
0.00009
cyclopropane-1,1-dicarboxylate
-
-
0.0000903
cyclopropane-1,1-dicarboxylate
-
pH 8.0, 30C, recombinant enzyme, versus hydroxypyruvate
0.076
cyclopropane-1,1-dicarboxylic acid
-
pH 8.0, 30C
0.000716
dimethylmalonate
-
pH 8.0, 30C, recombinant enzyme
0.035
ethyl [(2-chlorophenyl)(hydroxy)amino](oxo)acetate
-
-
0.049
ethyl [hydroxy(2-methylphenyl)amino](oxo)acetate
-
-
0.351
ethyl [hydroxy(4-methylphenyl)amino](oxo)acetate
-
-
1.704
ethyl [[4-(cyanomethyl)phenyl](hydroxy)amino](oxo)acetate
-
-
0.0025
ethylene glycol
-
pH 8.0, 30C, recombinant enzyme, competitive mode
0.0032
ethylene glycol
-
pH 8.0, 30C, recombinant enzyme, uncompetitive mode
0.0027
N-Hydroxy-N-isopropyloxamate
-
pH 8.0, 30C
0.00275
N-Hydroxy-N-isopropyloxamate
-
-
0.005
NADP+
-
pH 8.2, 30C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate
0.0075
NADP+
-
pH 8.2, 30C, NADPH as variable substrate, 0.2 mM (2S)-2-aceto-2-hydroxybutanoate as fixed substrate
0.225
NADP+
-
pH 8.2, 30C, (2S)-2-aceto-2-hydroxybutanoate as variable substrate, 0.075 mM NADPH as fixed substrate
0.33
NADP+
-
pH 8.2, 30C, (2S)-2-acetolactate as variable substrate, 0.075 mM NADPH as fixed substrate
0.0012
NADPH
-
pH 8.0, 22C, wild-type enzyme
0.0018
NADPH
-
pH 8.0, 22C, mutant enzyme K69L
0.0039
NADPH
-
pH 8.0, 22C, mutant enzyme K75Q
0.0085
NADPH
-
pH 8.0, 22C, mutant enzyme R68Q
0.0226
NADPH
-
pH 8.0, 22C, mutant enzyme K76Q
0.000058
1-cyano-cyclopropane carboxylate
-
-
additional information
1-cyano-N-(4-methylphenyl)cyclopropanecarboxamide
-
value above 300
0.034
methyl [hydroxy(1-methylethyl)amino](oxo)acetate
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
inhibition mechanism and kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
-
purified recombinant enzyme, substrate 2-acetolactate
1.9
-
purified enzyme
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
1.97
-
purified recombinant enzyme, substrate hydroxypyruvate
3
-
deletion mutant DELTA423-430/F431S
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
constant activity with 2-acetolactate as substrate
7.5
-
2-acetolactate as substrate; alpha-aceto-alpha-hydroxybutyrate
7.5
-
2-acetolactate as substrate
7.5 - 8
-
reaction with 2-acetolactate, isoenzyme 1
8 - 8.5
-
reaction with 2-aceto-2-hydroxybutyrate
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
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
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 - 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
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 4.7
-
chromatofocusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
germinating, with appressoria, high expression level
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A)
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1)
Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1)
Oryza sativa subsp. japonica
Oryza sativa subsp. japonica
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
-
monomeric mutant enzyme DELTA423-431/F431S, gel filtration
639185
110000
-
dimeric wild-type enzyme, gel filtration
639185
115000
-
recombinant enzyme expressed in E. coli, gel filtration
639179
115000
-
gel filtration
639180
205000
-
SDS-PAGE, isoenzyme 3
639176
205000
-
non-denaturing SDS-PAGE
639179
220000
-
sedimentation equilibrium centrifugation
639169, 639174
220000
-
SDS-PAGE, isoenzyme 2
639176
228000
sedimentation equilibrium analysis
725718
230000
gel filtration
725718
235000
-
SDS-PAGE, isoenzyme 1
639176
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
639184
266000
-
native molecular mass
654058
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 55000, SDS-PAGE
dimer
-
2 * 56850, calculation from acid sequence; 2 * 57000, SDS-PAGE
dimer
-
2 * 59000, SDS-PAGE
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
dimer
-
structure-function relationship, effects of ligand, Mg2+ and NADPH, binding on the enzyme conformation, overview
homohexamer
-
-
tetramer
-
4 * 57000, equilibrium sedimentation after treatment with 0.1 M 2-mercaptoethanol and 6 M guanidine hydrochloride
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
three-dimensional enzyme structure, subunit domain structures, surface contact and interlock, crystal structure analysis, overview
tetramer
4 * 52428, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
purified enzyme contains 39-46% lipid
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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, 17C, 6 months, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
the enzyme is remarkably easy to crystallize
-
enzyme KARI in complex with Mg2+ or with Mg2+ and NADPH, hanging-drop method by vaporphase diffusion at 18C, 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
-
X-ray, structure analysis
-
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
-
crystallized with 2-aceto-2-hydroxybutanoate, Mn2+ and NADPH
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
-
40C, 5 min, 90% loss of activity
639171
6.5
-
40C, 5 min, 55% loss of activity
639171
7
-
40C, 5 min, 35% loss of activity
639171
7.5
-
40C, 5 min, 30% loss of activity
639171
8
-
40C, 5 min, 85% loss of activity
639171
8.5
-
40C, 5 min, 90% loss of activity
639171
10
-
rapid loss of activity above pH 10 with 2-acetolactate as substrate
639178
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
639171
additional information
-
deletion mutant DELTA423-4301/F431S shows significantly lower temperature stability than wild type enzyme
639185
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in absence of NADPH and Mg2+, very unstable in Tris buffer, 2-mercaptoethanol stabilizes
-
high activity loss during DEAE-cellulose chromatography, stable towards acetone fractionation and dialysis, unstable towards freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10, in presence of NADPH, 5 d, 70-80% loss of activity
-
-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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
of wild-type and mutants
-
recombinant His6-tagged enzyme
-
wild-type and mutant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
-
mutant enzyme DELTA423-431/F431S; recombinant enzyme from Escherichia coli
-
recombinant enzyme from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ilvC expression in Escherichia coli using an Escherichia coli-Corynebacterium glutamicum shuttle vector pECKA
-
expression as His6-tagged enzyme
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
overexpression in Escherichia coli strain BL21(DE3)
-
gene Pi-kari1, quantitative expression analysis
-
expression in Escherichia coli
-
expressd in Escherichia coli and Saccharomyces cerevisiae
-
expression in Escherichia coli
-
mutant enzyme DELTA423-431/F431S, expression in Escherichia coli
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D217E
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
D217N
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E213D
-
75% reductoisomerase activity in comparison of 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
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
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mutant with N-terminal 53-residue deletion: cellular localisation throughout the cytosol rather than in mitochondria
DELTA1-66
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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
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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
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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
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 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