Aspartate—prephenate aminotransferase
| Aspartate-prephenate aminotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.78 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, aspartate-prephenate aminotransferase (EC 2.6.1.78) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-arogenic acid (shown in its carboxylate form) and oxaloacetic acid. Its products are prephenic acid and L-aspartic acid.[1][2]
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arogenate:oxaloacetate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase.
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