The enzyme(R)-2-methylmalate dehydratase (EC 4.2.1.35) catalyzes the chemical reaction
| (R)-2-methylmalate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.35 | ||||||||
| CAS no. | 9027-92-3 | ||||||||
| 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 | ||||||||
| |||||||||
- (R)-2-methylmalate 2-methylmaleate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (R)-2-methylmalate hydro-lyase (2-methylmaleate-forming). Other names in common use include citraconate hydratase, citraconase, citramalate hydro-lyase, (−)-citramalate hydro-lyase, and (R)-2-methylmalate hydro-lyase. This enzyme participates in valine, leucine and isoleucine biosynthesis and c5-branched dibasic acid metabolism. It employs one cofactor, iron.
References
edit- Subramanian SS, Rao MR (1968). "Purification and properties of citraconase". J. Biol. Chem. 243 (9): 2367–72. PMID 4296839.
