3-Isopropylmalate dehydratase
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 | |||||||||
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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 | ||||||||
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References
- 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.
External links
- 3-isopropylmalate+dehydratase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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