3-Isopropylmalate dehydratase (EC 4.2.1.33) is an aconitase homologue,[1][2][3] which catalyses the isomerisation of 2-isopropylmalate to 3-isopropylmalate, via dehydration, in the biosynthesis of leucine.
| 3-isopropylmalate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.33 | ||||||||
| CAS no. | 37290-72-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- ^ Gross SR, Burns RO, Umbarger HE (1963). “The biosynthesis of leucine. II. The enzymic isomerization of beta-carboxy-beta-hydroxyisocaproate and alpha-hydroxy-beta-carboxyisocaproate”. Biochemistry. 2 (5): 1046–52. doi:10.1021/bi00905a023. PMID 14087357.
- ^ Calvo JM, Stevens CM, Kalyanpur MG, Umbarger HE (December 1964). “The absolute configuration of alpha-hydroxy-beta-carboxyisocaproic acid (3-isopropylmalic acid), an intermediate in leucine biosynthesis”. Biochemistry. 3 (12): 2024–7. doi:10.1021/bi00900a043. PMID 14269331.
- ^ Cole FE, Kalyanpur MG, Stevens CM (August 1973). “Absolute configuration of alpha isopropylmalate and the mechanism of its conversion to beta isopropylmalate in the biosynthesis of leucine”. Biochemistry. 12 (17): 3346–50. doi:10.1021/bi00741a031. PMID 4270046.
- 3-isopropylmalate+dehydratase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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