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Information on EC 1.1.1.86 - ketol-acid reductoisomerase (NADP+) and Organism(s) Spinacia oleracea and UniProt Accession Q01292
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1.1.1.86 ketol-acid reductoisomerase (NADP+)IUBMB Comments
Also catalyses the reduction of 2-ethyl-2-hydroxy-3-oxobutanoate to 2,3-dihydroxy-3-methylpentanoate. The enzyme, found in many bacteria and archaea, is specific for NADPH (cf. EC 1.1.1.382, ketol-acid reductoisomerase (NAD+) and EC 1.1.1.383, ketol-acid reductoisomerase [NAD(P)+]).
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Word Map
- 1.1.1.86
-
branched-chain
- 5-phosphate
-
karis
- 1-deoxy-d-xylulose
- fosmidomycin
-
isoprenoids
- methylerythritol
- 1-deoxy-d-xylulose-5-phosphate
- deoxyxylulose
- l-valine
- isobutanol
-
2-c-methyl-d-erythritol
-
non-mevalonate
-
dihydroxyacid
-
2-keto
-
isoleucine-valine
-
ilvbnce
- drug development
- biofuel production
- industry
The taxonomic range for the selected organisms is: Spinacia oleracea
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
reductoisomerase, ketol-acid reductoisomerase, acetohydroxy acid isomeroreductase, ilv5p, isomeroreductase, acetohydroxyacid isomeroreductase, ahair, acetohydroxy acid reductoisomerase, ilvc1, acetolactate reductoisomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxy-3-keto acid reductoisomerase
-
-
-
-
acetohydroxy acid isomeroreductase
acetohydroxy acid reductoisomerase
-
-
-
-
acetohydroxy-acid isomeroreductase
-
-
-
-
acetohydroxy-acid reductoisomerase
-
-
-
-
acetolactate reductoisomerase
-
-
-
-
alpha-keto-beta-hydroxylacil reductoisomerase
-
-
-
-
alpha-keto-beta-hydroxylacyl reductoisomerase
-
-
-
-
dehydrogenase, dihydroxyisovalerate (isomerizing)
-
-
-
-
dihydroxyisovalerate dehydrogenase (isomerizing)
-
-
-
-
isomerase, ketol acid reducto-
-
-
-
-
isomeroreductase
-
-
-
-
KARI
reductoisomerase
-
-
-
-
acetohydroxy acid isomeroreductase
-
-
-
-
KARI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
rearrangement
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -
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)+]).
CAS REGISTRY NUMBER
COMMENTARY
9075-02-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
enzyme of branched chain amino acid synthesis
-
r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
?
2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+ + H+
-
-
-
-
r
NADPH + 2-acetolactate
NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate
-
-
-
-
?
additional information
?
-
-
structure-biological activity relationship, overview
-
-
?
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
enzyme of branched chain amino acid synthesis
-
r
additional information
?
-
-
structure-biological activity relationship, overview
-
-
?
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
2-acetolactate + NADPH
2,3-dihydroxy-3-methylbutanoate + NADP+
-
enzyme of branched chain amino acid synthesis
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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-dimethylphosphinoyl-2-hydroxyacetate
-
i.e. Hoe 704, potent competitive inhibitor in vitro but weak in vivo
N-(4-chlorophenyl)-1-cyanocyclopropanecarboxamide
-
inhibition rate: 93.92%
2-dimethylphosphinoyl-2-hydroxyacetic acid
-
reversible, strong competitive inhibition
N-Hydroxy-N-isopropyloxamate
-
i.e. IpOHA, potent competitive inhibitor in vitro but weak in vivo
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
-
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
0.007
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
1-cyano-N-(4-methylphenyl)cyclopropanecarboxamide
-
value above 300
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
0.24
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
0.005
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
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
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
7 - 8.5
-
pH 7.0: about 25% of maximal activity, pH 8.0-8.5: optimum, isoenzyme 1
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
one of the key enzymes for the synthesis of branched-chain amino acids isoleucine, leucine and valine
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ILV5_SPIOL
595
0
63754
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
deletion mutant DELTA423-4301/F431S shows significantly lower temperature stability than wild type enzyme
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
-
the enzyme is a promising target for the design of herbicides
drug development
-
the enzyme is a target for herbicide drug development, computer-aided drug design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dumas, R.; Joyard, J.; Douce, R.
Purification and characterization of acetohydroxyacid reductoisomerase from spinach chloroplasts
Biochem. J.
262
971-976
1989
Spinacia oleracea
Dumas, R.; Job, D.; Ortholand, J.Y.; Emeric, G.; Greiner, A.; Douce, R.
Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli
Biochem. J.
288
865-874
1992
Spinacia oleracea
-
Dumas, R.; Cornillon-Bertrand, C.; Guigue-Talet, P.; Genix, P.; Douce, R.; Job, D.
Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogues: correlation of the slow, competitive, inhibition kinetics of enzyme activity and herbicidal effects
Biochem. J.
301
813-820
1994
Ipomoea purpurea, Solanum nigrum, Spinacia oleracea
-
Biou, V.; Dumas, R.; Cohen-Addad, C.; Douce, R.; Job, D.; Pebay-Peyroula, E.
The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution
EMBO J.
16
3405-3415
1997
Spinacia oleracea
Dumas, R.; Biou, V.; Douce, R.
Purification and characterization of a fusion protein of plant acetohydroxy acid synthase and acetohydroxy acid isomeroreductase
FEBS Lett.
408
156-160
1997
Spinacia oleracea
Wessel, P.M.; Biou, V.; Douce, R.; Dumas, R.
A loop deletion in the plant acetohydroxy acid isomeroreductase homodimer generates an active monomer with reduced stability and altered magnesium affinity
Biochemistry
37
12753-12760
1998
Spinacia oleracea
Thomazeau, K.; Dumas, R.; Halgand, F.; Forest, E.; Douce, R.; Biou, V.
Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose
Acta Crystallogr. Sect. D
56
389-397
2000
Spinacia oleracea
-
Dumas, R.; Biou, V.; Halgand, F.; Douce, R.; Duggleby, R.G.
Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase
Acc. Chem. Res.
34
399-408
2001
Escherichia coli, Triticum aestivum, Spinacia oleracea (Q01292)
Liu, X.H.; Chen, P.Q.; Wang, B.L.; Li, Y.H.; Wang, S.H.; Li, Z.M.
Synthesis, bioactivity, theoretical and molecular docking study of 1-cyano-N-substituted-cyclopropanecarboxamide as ketol-acid reductoisomerase inhibitor
Bioorg. Med. Chem. Lett.
17
3784-3788
2007
Spinacia oleracea
Wang, B.; Li, Y.; Wang, J.; Ma, Y.; Li, Z.
Molecular design, synthesis and biological activities of amidines as new ketol-acid reductoisomerase inhibitors
Chin. Chem. Lett.
19
651-654
2008
Escherichia coli, Oryza sativa, Spinacia oleracea
-
Wang, B.; Ma, Y.; Li, Y.; Wang, S.; Li, Z.
The design, synthesis of amide KARI inhibitors and their biological activities
Front. Chem. Chin.
4
186-190
2009
Spinacia oleracea
-
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