2-aminoethylphosphonate-pyruvate transaminase

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In enzymology, a 2-aminoethylphosphonate-pyruvate transaminase (EC 2.6.1.37) is an enzyme that catalyzes the chemical reaction

(2-aminoethyl)phosphonate + pyruvate $\rightleftharpoons$ 2-phosphonoacetaldehyde + L-alanine

Thus, the two substrates of this enzyme are (2-aminoethyl)phosphonate and pyruvate, whereas its two products are 2-phosphonoacetaldehyde and L-alanine.

This enzyme belongs to the family of transferases, specifically the transaminases, 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 employs one cofactor, pyridoxal phosphate.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1M32.

[edit] References

IUBMB entry for 2.6.1.37
BRENDA references for 2.6.1.37 (Recommended.)
PubMed references for 2.6.1.37
PubMed Central references for 2.6.1.37
Google Scholar references for 2.6.1.37
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. PMID 4982500.
Dumora C, Lacoste AM, Cassaigne A (1983). "Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa". Eur. J. Biochem. 133: 119–25. doi:10.1111/j.1432-1033.1983.tb07436.x. PMID 6406228.
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. doi:10.1111/j.1432-1033.1993.tb18100.x. PMID 8394813.
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. PMID 1527499.