ExplorEnz: EC 4.2.1.33

Your query returned 1 entry. Printable version

4.2.1.33

Accepted name:

3-isopropylmalate dehydratase

Reaction:

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate (overall reaction)
(1a) (2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H₂O
(1b) 2-isopropylmaleate + H₂O = (2S)-2-isopropylmalate

For diagram of leucine biosynthesis, click here

Glossary:

α-isopropylmalate = (2S)-2-isopropylmalate
β-isopropylmalate = (2R,3S)-3-isopropylmalate

Other name(s):

(2R,3S)-3-isopropylmalate hydro-lyase; β-isopropylmalate dehydratase; isopropylmalate isomerase; α-isopropylmalate isomerase; 3-isopropylmalate hydro-lyase

Systematic name:

(2R,3S)-3-isopropylmalate hydro-lyase (2-isopropylmaleate-forming)

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:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37290-72-5

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 (1963) 1046–1052. [PMID: 14087357]
2.	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 3 (1964) 2024–2027. [PMID: 14269331]
3.	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 (1973) 3346–3350. [PMID: 4270046]
4.	Jang, S. and Imlay, J.A. Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J. Biol. Chem. 282 (2007) 929–937. [DOI] [PMID: 17102132]

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