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Information on EC 1.1.1.86 - ketol-acid reductoisomerase (NADP+) and Organism(s) Azotobacter vinelandii and UniProt Accession C1DFH7

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EC Tree
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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This record set is specific for:
Azotobacter vinelandii
UNIPROT: C1DFH7
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Word Map
The taxonomic range for the selected organisms is: Azotobacter vinelandii
The enzyme appears in selected viruses and cellular organisms
Synonyms
reductoisomerase, ketol-acid reductoisomerase, acetohydroxy acid isomeroreductase, ilv5p, isomeroreductase, acetohydroxyacid isomeroreductase, ahair, acetohydroxy acid reductoisomerase, ilvc1, acetolactate reductoisomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetohydroxyacid isomeroreductase
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2-hydroxy-3-keto acid reductoisomerase
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acetohydroxy acid isomeroreductase
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acetohydroxy acid reductoisomerase
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acetohydroxy-acid isomeroreductase
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acetohydroxy-acid reductoisomerase
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acetolactate reductoisomerase
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alpha-keto-beta-hydroxylacil reductoisomerase
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alpha-keto-beta-hydroxylacyl reductoisomerase
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dehydrogenase, dihydroxyisovalerate (isomerizing)
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dihydroxyisovalerate dehydrogenase (isomerizing)
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isomerase, ketol acid reducto-
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isomeroreductase
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KARI
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reductoisomerase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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rearrangement
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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)+]).
CAS REGISTRY NUMBER
COMMENTARY hide
9075-02-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
show the reaction diagram
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-
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r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
show the reaction diagram
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r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-2-acetolactate + NADH + H+
(R)-2,3-dihydroxyisovalerate + NAD+
show the reaction diagram
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r
(S)-2-acetolactate + NADPH + H+
(R)-2,3-dihydroxyisovalerate + NADP+
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cahn, J.K.; Brinkmann-Chen, S.; Spatzal, T.; Wiig, J.A.; Buller, A.R.; Einsle, O.; Hu, Y.; Ribbe, M.W.; Arnold, F.H.
Cofactor specificity motifs and the induced fit mechanism in Class I ketol-acid reductoisomerases
Biochem. J.
468
475-484
2015
Alicyclobacillus acidocaldarius subsp. acidocaldarius (C8WR67), Azotobacter vinelandii (C1DFH7), Azotobacter vinelandii ATCC BAA-1303 (C1DFH7), Ignisphaera aggregans (E0SRA9), Ignisphaera aggregans DSM 17230 (E0SRA9), uncultured archaeon (Q64BR7)
Manually annotated by BRENDA team