| taurine-2-oxoglutarate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.55 | ||||||||
| CAS no. | 9076-52-2 | ||||||||
| 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, a taurine-2-oxoglutarate transaminase (EC 2.6.1.55) is an enzyme that catalyzes the chemical reaction.
- taurine + 2-oxoglutarate sulfoacetaldehyde + L-glutamate
Thus, the two substrates of this enzyme are taurine and 2-oxoglutarate, whereas its two products are sulfoacetaldehyde 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 taurine:2-oxoglutarate aminotransferase. Other names in common use include taurine aminotransferase, taurine transaminase, taurine-alpha-ketoglutarate aminotransferase, and taurine-glutamate transaminase. This enzyme participates in beta-alanine metabolism. It employs one cofactor, pyridoxal phosphate.
References
- Toyama S, Misono H, Soda K (1972). "Crystalline taurine: -ketoglutarate aminotransferase from Achromobacter superficialis". Biochem. Biophys. Res. Commun. 46 (3): 1374–9. doi:10.1016/S0006-291X(72)80127-X. PMID 5012173.
- Cook AM, Denger K (2002). "Dissimilation of the C2 sulfonates". Arch. Microbiol. 179 (1): 1–6. doi:10.1007/s00203-002-0497-0. PMID 12471498.
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