Biology:Taurine—2-oxoglutarate transaminase
From HandWiki
| Taurine-2-oxoglutarate transaminase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.6.1.55 | ||||||||
| CAS number | 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 | ||||||||
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Taurine-2-oxoglutarate transaminase (EC 2.6.1.55) is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction.
- REDIRECT Template:Chemical reaction
The two substrates of this enzyme characterised from Achromobacter superficialis are taurine and α-ketoglutaric acid. Its products are sulfoacetaldehyde and L-glutamic acid.[1][2]
This enzyme is a transferase, specifically a transaminase, 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. It participates in beta-alanine metabolism.[3]
References
- ↑ "Crystalline taurine: -ketoglutarate aminotransferase from Achromobacter superficialis". Biochem. Biophys. Res. Commun. 46 (3): 1374–9. 1972. doi:10.1016/S0006-291X(72)80127-X. PMID 5012173.
- ↑ "Dissimilation of the C2 sulfonates". Arch. Microbiol. 179 (1): 1–6. 2002. doi:10.1007/s00203-002-0497-0. PMID 12471498. http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-67394.
- ↑ Enzyme 2.6.1.55 at KEGG Pathway Database.
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