2-aminoethylphosphonate—pyruvate transaminase
| 2-aminoethylphosphonate-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.37 | ||||||||
| CAS no. | 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.
