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, an aspartate-prephenate aminotransferase (EC 2.6.1.78) is an enzyme that catalyzes the chemical reaction
- L-arogenate + oxaloacetate prephenate + L-aspartate
Thus, the two substrates of this enzyme are L-arogenate and oxaloacetate, whereas its two products are prephenate and L-aspartate.
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.
References
[edit]- De-Eknamkul W, Ellis BE (1988). "Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures". Arch. Biochem. Biophys. 267 (1): 87–94. doi:10.1016/0003-9861(88)90011-2. PMID 3196038.
