2-aminoethylphosphonate—pyruvate transaminase () is an enzyme originally characterised from Bacillus cereus that catalyzes a reversible chemical reaction that interconverts 2-aminoethylphosphonic acid and pyruvic acid with phosphonoacetaldehyde and L-alanine. It has also been found in Pseudomonas aeruginosa. In that case, 2-aminoethylarsonate can replace 2-aminoethylphosphonic acid.
The enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is (2-aminoethyl)phosphonate:pyruvate aminotransferase. Other names in common use include (2-aminoethyl)phosphonate transaminase, (2-aminoethyl)phosphonate aminotransferase, (2-aminoethyl)phosphonic acid aminotransferase, 2-aminoethylphosphonate-pyruvate aminotransferase, 2-aminoethylphosphonate aminotransferase, 2-aminoethylphosphonate transaminase, AEP transaminase, and AEPT. This enzyme participates in aminophosphonate metabolism. It uses pyridoxal phosphate and the stereochemistry of the interaction between 2-aminoethylphosphonic acid and that cofactor has been determined.
Structural studies As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
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