2-aminoethylphosphonate—pyruvate transaminase

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2-aminoethylphosphonate-pyruvate transaminase
Identifiers
EC number 2.6.1.37
CAS number 37277-91-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

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

(2-aminoethyl)phosphonate + pyruvate 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.

Structural studies[edit]

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

References[edit]

  • 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 (3): 438–47. doi:10.1016/0304-4165(68)90223-7. PMID 4982500. 
  • Dumora C, Lacoste AM, Cassaigne A (1983). "Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa". Eur. J. Biochem. 133 (1): 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 (3): 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 (6): 1283–7. doi:10.1099/00221287-138-6-1283. PMID 1527499.