| aromatic-amino-acid transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.57 | ||||||||
| CAS no. | 37332-38-0 | ||||||||
| 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 aromatic-amino-acid transaminase ( EC 2.6.1.57) is an enzyme that catalyzes the chemical reaction
- an aromatic amino acid + 2-oxoglutarate an aromatic oxo acid + L-glutamate
Thus, the two substrates of this enzyme are aromatic amino acid and 2-oxoglutarate, whereas its two products are aromatic oxo acid and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is aromatic-amino-acid:2-oxoglutarate aminotransferase. Other names in common use include aromatic amino acid aminotransferase, aromatic aminotransferase, and ArAT. This enzyme participates in 6 metabolic pathways: methionine metabolism, tyrosine metabolism, phenylalanine metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, novobiocin biosynthesis, and alkaloid biosynthesis i. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1AY4, 1AY5, 1AY8, 2AY1, 2AY2, 2AY3, 2AY4, 2AY5, 2AY6, 2AY7, 2AY8, 2AY9, and 3TAT.
References
- Mavrides C, Orr W (1975). "Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli". J. Biol. Chem. 250 (11): 4128–33. PMID 236311.
