Citramalate lyase
From Wikipedia, the free encyclopedia
In enzymology, a citramalate lyase (EC 4.1.3.22) is an enzyme that catalyzes the chemical reaction
- (2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
Hence, this enzyme has one substrate, (2S)-2-hydroxy-2-methylbutanedioate, and two products, acetate and pyruvate.
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.
[edit] References
- IUBMB entry for 4.1.3.22
- BRENDA references for 4.1.3.22 (Recommended.)
- PubMed references for 4.1.3.22
- PubMed Central references for 4.1.3.22
- Google Scholar references for 4.1.3.22
- Barker HA (1967). "Citramalate lyase of Clostridium tetanomorphum". Arch. Mikrobiol. 59: 4–12. doi:. 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: 469–77. doi:. PMID 923590.
[edit] External links
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- The CAS registry number for this enzyme class is 9027-93-4.

