Summary
In enzymology, a tryptophan transaminase (EC 2.6.1.27) is an enzyme that catalyzes the chemical reaction
| tryptophan transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 L-tryptophan aminotransferase dimer, Arabidopsis thaliana | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.27 | ||||||||
| CAS no. | 9022-98-4 | ||||||||
| 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 | ||||||||
| |||||||||
- L-tryptophan + 2-oxoglutarate (indol-3-yl)pyruvate + L-glutamate
Thus, the two substrates of this enzyme are L-tryptophan and 2-oxoglutarate, whereas its two products are (indol-3-yl)pyruvate 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 L-tryptophan:2-oxoglutarate aminotransferase. Other names in common use include L-phenylalanine-2-oxoglutarate aminotransferase, tryptophan aminotransferase, 5-hydroxytryptophan-ketoglutaric transaminase, hydroxytryptophan aminotransferase, L-tryptophan aminotransferase, and L-tryptophan transaminase. This enzyme participates in tryptophan metabolism. It employs one cofactor, pyridoxal phosphate.
References edit
- George H, Gabay S (1968). "Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase". Biochim. Biophys. Acta. 167 (3): 555–66. doi:10.1016/0005-2744(68)90045-4. PMID 5722279.
- O'Neil SR, DeMoss RD (1968). "Tryptophan transaminase from Clostridium sporogenes". Arch. Biochem. Biophys. 127 (1): 361–9. doi:10.1016/0003-9861(68)90237-3. PMID 5697992.
- Tangen O; Fonnum F; Haavaldsen R (1965). "Separation and purification of aromatic amino acid transaminases from rat brain". Biochim. Biophys. Acta. 96: 82–90. doi:10.1016/0005-2787(65)90612-x. PMID 14285270.
