(S)-2-methylmalate dehydratase
(S)-2-methylmalate dehydratase | |||||||||
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Identifiers | |||||||||
EC number | 4.2.1.34 | ||||||||
CAS number | 9027-94-5 | ||||||||
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 / EGO | ||||||||
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In enzymology, a (S)-2-methylmalate dehydratase (EC 4.2.1.34) is an enzyme that catalyzes the chemical reaction
- (S)-2-methylmalate 2-methylfumarate + H2O
Hence, this enzyme has one substrate, (S)-2-methylmalate, and two products, 2-methylfumarate and 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 (S)-2-methylmalate hydro-lyase (2-methylfumarate-forming). Other names in common use include mesaconate hydratase, (+)-citramalate hydro-lyase, L-citramalate hydrolase, citramalate dehydratase, (+)-citramalic hydro-lyase, mesaconate mesaconase, mesaconase, and (S)-2-methylmalate hydro-lyase. This enzyme participates in c5-branched dibasic acid metabolism.
References
- Blair AH, Barker HA (1966). "Assay and purification of (+)-citramalate hydro-lyase components from Clostridium tetanomorphum". J. Biol. Chem. 241 (2): 400–8. PMID 5903732.
- Wang CC, Barker HA (1969). "Purification and properties of L-citramalate hydrolyase". J. Biol. Chem. 244 (10): 2516–26. PMID 5769987.
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