Beta-alanine-pyruvate transaminase
In enzymology, a beta-alanine-pyruvate transaminase (EC 2.6.1.18) is an enzyme that catalyzes the chemical reaction
- L-alanine + 3-oxopropanoate <math>\rightleftharpoons</math> pyruvate + beta-alanine
Thus, the two substrates of this enzyme are L-alanine and 3-oxopropanoate, whereas its two products are pyruvate and beta-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:3-oxopropanoate aminotransferase. Other names in common use include beta-alanine-pyruvate aminotransferase, and beta-alanine-alpha-alanine transaminase. This enzyme participates in 4 metabolic pathways: alanine and aspartate metabolism, valine, leucine and isoleucine degradation, beta-alanine metabolism, and propanoate metabolism. It employs one cofactor, pyridoxal phosphate.
References
- IUBMB entry for 2.6.1.18
- BRENDA references for 2.6.1.18 (Recommended.)
- PubMed references for 2.6.1.18
- PubMed Central references for 2.6.1.18
- Google Scholar references for 2.6.1.18
- HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S (1961). "Enzymatic studies on the metabolism of beta-alanine". J. Biol. Chem. 236: 781–90. PMID 13712439.
- Stinson RA, Spencer MS (1969). "Beta alanine aminotransferase (s) from a plant source". Biochem. Biophys. Res. Commun. 34: 120–7. PMID 5762452.
External links
- The CAS registry number for this enzyme class is 9030-47-1.
Gene Ontology (GO) codes
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