2-aminoethylphosphonate—pyruvate transaminase

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
2-aminoethylphosphonate-pyruvate transaminase
Identifiers
EC no.2.6.1.37
CAS no.37277-91-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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

References

    • 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.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.