Aspartate—phenylpyruvate transaminase
(Redirected from EC 2.6.1.70)
| aspartate-phenylpyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.70 | ||||||||
| CAS no. | 99533-45-6 | ||||||||
| 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, an aspartate-phenylpyruvate transaminase (EC 2.6.1.70) is an enzyme that catalyzes the chemical reaction
- L-aspartate + phenylpyruvate oxaloacetate + L-phenylalanine
Thus, the two substrates of this enzyme are L-aspartate and phenylpyruvate, whereas its two products are oxaloacetate and L-phenylalanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-aspartate:phenylpyruvate aminotransferase. This enzyme is also called aspartate-phenylpyruvate aminotransferase.
References[edit]
- Holger Z, Kula MR (1985). "Isolation and characterization of a highly inducible L-aspartate-phenylpyruvate transaminase from Pseudomonas putida". J. Biotechnol. 3: 19–31. doi:10.1016/0168-1656(85)90004-5.
