Tryptophan transaminase
| Tryptophan transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 L-tryptophan aminotransferase dimer, Arabidopsis thaliana | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.27 | ||||||||
| CAS no. | 9022-98-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Tryptophan transaminase (EC 2.6.1.27) is an enzyme originally characterised from rat brain that catalyzes a reversible chemical reaction that interconverts L-tryptophan and α-ketoglutaric acid with indole-3-pyruvic acid and L-glutamic acid.[1] It has also been found in pig brain and the bacterium Clostridium sporogenes.[2][3] The structure of the enzyme from Arabidopsis thaliana has been determined by X-ray crystallography.[4]
This enzyme is a transferase, specifically a transaminase, 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 and uses pyridoxal phosphate as a cofactor.[5]
References
- ↑ 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.
- ↑ 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.
- ↑ Ferrer, J.-L.; Noel, J.P.; Pojer, F.; Bowman, M.; Chory, J.; Tao, Y. (2008). "L-tryptophan aminotransferase". Protein data bank. doi:10.2210/pdb3BWN/pdb.
- ↑ Enzyme 2.6.1.27 at KEGG Pathway Database.