2-aminoethylphosphonate—pyruvate transaminase

InterPro Family 2-aminoethylphosphonate-pyruvate transaminase 2.6.1.37 37277-91-1 0047304 2-aminoethylphosphonate—pyruvate transaminase (2.6.1.37) 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.La Nauze JM, Rosenberg H 1968 The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus Biochim. Biophys. Acta 165 438–47 4982500 3 10.1016/0304-4165(68)90223-7 It has also been found in Pseudomonas aeruginosa. In that case, 2-aminoethylarsonate can replace 2-aminoethylphosphonic acid.Dumora C, Lacoste AM, Cassaigne A 1983 Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa Eur. J. Biochem. 133 119–25 6406228 10.1111/j.1432-1033.1983.tb07436.x 1 free Lacoste AM, Dumora C, Ali BR, Neuzil E, Dixon HB 1992 Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa J. Gen. Microbiol. 138 1283–7 1527499 6 10.1099/00221287-138-6-1283 free 65% Q421682 2-aminoethylphosphonic acid + pyruvic acid reversible Q27094110 phosphonoacetaldehyde + alanine 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.2.6.1.37 It uses pyridoxal phosphate and the stereochemistry of the interaction between 2-aminoethylphosphonic acid and that cofactor has been determined.Lacoste AM, Dumora C, Balas L, Hammerschmidt F, Vercauteren J 1993 Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase. A 1H-NMR study Eur. J. Biochem. 215 841–4 8394813 10.1111/j.1432-1033.1993.tb18100.x free 3 Structural studies As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1M32. References Biology no Category:EC 2.6.1 Category:Pyridoxal phosphate enzymes Category:Enzymes of known structure