| 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-aminoethylphosphonateâpyruvate 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
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): 438â47. 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): 119â25. 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): 841â4. 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): 1283â7. doi: 10.1099/00221287-138-6-1283. PMID 1527499.
| 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-aminoethylphosphonateâpyruvate 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
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): 438â47. 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): 119â25. 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): 841â4. 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): 1283â7. doi: 10.1099/00221287-138-6-1283. PMID 1527499.