Aspartate—phenylpyruvate transaminase
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
- Holger Z and Kula M-R (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.
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