Citramalate lyase
The enzyme citramalate lyase (EC 4.1.3.22) catalyzes the chemical reaction
- (2S)-2-hydroxy-2-methylbutanedioate acetate + pyruvate
citramalate lyase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.3.22 | ||||||||
CAS no. | 9027-93-4 | ||||||||
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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This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase (acetate-forming). Other names in common use include citramalate pyruvate-lyase, citramalate synthase, citramalic-condensing enzyme, citramalate synthetase, citramalic synthase, (S)-citramalate lyase, (+)-citramalate pyruvate-lyase, citramalate pyruvate lyase, (3S)-citramalate pyruvate-lyase, and (2S)-2-hydroxy-2-methylbutanedioate pyruvate-lyase. This enzyme participates in c5-branched dibasic acid metabolism.
References
- Barker HA (1967). "Citramalate lyase of Clostridium tetanomorphum". Arch. Mikrobiol. 59 (1): 4–12. doi:10.1007/BF00406311. PMID 4301387.
- Dimroth P, Buckel W, Loyal R, Eggerer H (1977). "Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase". Eur. J. Biochem. 80 (2): 469–77. doi:10.1111/j.1432-1033.1977.tb11902.x. PMID 923590.
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