EC 4.2.1.33 - 3-isopropylmalate dehydratase

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IntEnz Enzyme Nomenclature
EC 4.2.1.33

Names

Accepted name:
3-isopropylmalate dehydratase
Other names:
α-isopropylmalate isomerase
β-Isopropylmalate dehydratase
isopropylmalate isomerase
α-IPM isomerase
(2R,3S)-3-isopropylmalate hydro-lyase
3-isopropylmalate hydro-lyase
Systematic name:
(2R,3S)-3-isopropylmalate hydro-lyase (2-isopropylmaleate-forming)

Reactions

Cofactor

Comments:

Forms part of the leucine-biosynthesis pathway. The enzyme brings about the interconversion of the two isomers of isopropylmalate. It contains an iron-sulfur cluster.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00423
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003861
CAS Registry Number: 37290-72-5
UniProtKB/Swiss-Prot: (1077) [show] [UniProt]

References

  1. Gross, S.R., Burns, R.O. and Umbarger, H.E.
    The biosynthesis of leucine. II. The enzymic isomerization of β-carboxy-β-hydroxyisocaproate and α-hydroxy-β-carboxyisocaproate.
    Biochemistry 2: 1046-1052 (1963). [PMID: 14087357]
  2. Cole, F.E., Kalyanpur, M.G. and Stevens, C.M.
    Absolute configuration of α isopropylmalate and the mechanism of its conversion to β isopropylmalate in the biosynthesis of leucine.
    Biochemistry 12: 3346-3350 (1973). [PMID: 4270046]
  3. Calvo, J.M., Stevens, C.M., Kalyanpur, M.G. and Umbarger, H.E.
    The absolute configuration of α-hydroxy-β-carboxyisocaproic acid (3-isopropylmalic acid), an intermediate in leucine biosynthesis.
    Biochemistry 19: 2024-2027 (1964). [PMID: 14269331]
  4. Jang, S., Imlay, J. A.
    Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes.
    J. Biol. Chem. 282: 929-937 (2007). [PMID: 17102132]

[EC 4.2.1.33 created 1972, modified 1976, modified 2012]