EC 1.1.1.85 - 3-isopropylmalate dehydrogenase

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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
Systematic name:
(2R,3S)-3-isopropylmalate:NAD+ oxidoreductase

Reactions

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
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003862
CAS Registry Number: 9030-97-1
UniProtKB/Swiss-Prot: (302) [show] [UniProt]

References

  1. Burns, R.O., Umbarger, H.E. and Gross, S.R.
    The biosynthesis of leucine. III. The conversion of α-hydroxy-β-carboxyisocaproate to α-ketoisocaproate.
    Biochemistry 2: 1053 (1963). [PMID: 14087358]
  2. Parsons, S.J. and Burns, R.O.
    Purification and properties of β-isopropylmalate dehydrogenase.
    J. Biol. Chem. 244: 996-1003 (1969). [PMID: 4889950]
  3. Németh, A., Svingor, Á., Pócsik, M., Dobó, J., Magyar, C., Szilagyi, A., Gál, P., Závodszky, P.
    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]
  4. Calvo, J.M., Stevens, C.M., Kalyanpur, M.G. and Umbarger, H.E.
    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]