Beta-alanine-pyruvate transaminase () is an enzyme that catalyzes the reversible chemical reaction
The two substrates of this enzyme first characterised from Pseudomonas fluorescens are L-alanine and 3-oxopropanoic acid. Its products are pyruvic acid and β-alanine.
This enzyme is a transferase, specifically a transaminase, 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. It participates in four metabolic pathways: alanine and aspartate metabolism, valine, leucine and isoleucine degradation, beta-alanine metabolism, and propanoate metabolism. It uses pyridoxal phosphate as a cofactor.
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