Beta-alanine—pyruvate transaminase

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beta-alanine-pyruvate transaminase
Beta-alanine-pyruvate transaminase homotetramer, Pseudomonas aeruginosa
EC no.
CAS no.9030-47-1
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

L-alanine + 3-oxopropanoate 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.


  • 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 (1): 120–7. doi:10.1016/0006-291X(69)90537-3. PMID 5762452.