Beta-alanine-pyruvate transaminase

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In enzymology, a beta-alanine-pyruvate transaminase (EC 2.6.1.18) is an enzyme that catalyzes the chemical reaction

L-alanine + 3-oxopropanoate $\rightleftharpoons$ 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.

[edit] 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.