EC 1 - Oxidoreductases
EC 1.1 - Acting on the CH-OH group of donors
EC 1.1.1 - With NAD+ or NADP+ as acceptor
EC 1.1.1.85 - 3-isopropylmalate dehydrogenase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.1.1.85
Names
Accepted name:
3-isopropylmalate dehydrogenase
Other
names:
3-carboxy-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase
β-isopropylmalate dehydrogenase
β-isopropylmalic enzyme
threo-Ds-3-isopropylmalate dehydrogenase
IMDH
IPMDH
β-IPM dehydrogenase
β-isopropylmalate dehydrogenase
β-isopropylmalic enzyme
threo-Ds-3-isopropylmalate dehydrogenase
IMDH
IPMDH
β-IPM dehydrogenase
Systematic name:
(2R,3S)-3-isopropylmalate:NAD+ oxidoreductase
Reactions
- (1) (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH + H+
- (1a) (2R,3S)-3-isopropylmalate + NAD+ = (2S)-2-isopropyl-3-oxosuccinate + NADH + H+
- (1b) (2S)-2-isopropyl-3-oxosuccinate = 4-methyl-2-oxopentanoate + CO2 (spontaneous)
Comments:
The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Protein domains and families:
PROSITE:PDOC00389
Gene Ontology:
GO:0003862
CAS Registry Number:
9030-97-1
References
-
The biosynthesis of leucine. III. The conversion of α-hydroxy-β-carboxyisocaproate to α-ketoisocaproate.Biochemistry 2 : 1053 (1963). [PMID: 14087358]
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Purification and properties of β-isopropylmalate dehydrogenase.J. Biol. Chem. 244 : 996-1003 (1969). [PMID: 4889950]
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Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase.FEBS Lett. 468 : 48-52 (2000). [PMID: 10683439]
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The absolute configuration of alpha-hydroxy-beta-carboxyisocaproic acid (3-isopropylmalic acid), an intermediate in leucine biosynthesis.Biochemistry 3 : 2024-2027 (1964). [PMID: 14269331]
[EC 1.1.1.85 created 1972, modified 1976]