| cysteine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.3 | ||||||||
| CAS no. | 9030-32-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a cysteine transaminase ( EC 2.6.1.3) is an enzyme that catalyzes the chemical reaction
- L-cysteine + 2-oxoglutarate mercaptopyruvate + L-glutamate
Thus, the two substrates of this enzyme are L-cysteine and 2-oxoglutarate, whereas its two products are mercaptopyruvate 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-cysteine:2-oxoglutarate aminotransferase. Other names in common use include cysteine aminotransferase, L-cysteine aminotransferase, and CGT. This enzyme participates in cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
References
- CHATAGNER F, SAURET-IGNAZI G (June 1956). "[Role of transamination and pyridoxal phosphate in the enzymatic formation of hydrogen sulfide from cysteine by the rat liver under anaerobiosis.]". Bull. Soc. Chim. Biol. 38 (2–3). Paris: 415–28. PMID 13342749.
| cysteine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.3 | ||||||||
| CAS no. | 9030-32-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a cysteine transaminase ( EC 2.6.1.3) is an enzyme that catalyzes the chemical reaction
- L-cysteine + 2-oxoglutarate mercaptopyruvate + L-glutamate
Thus, the two substrates of this enzyme are L-cysteine and 2-oxoglutarate, whereas its two products are mercaptopyruvate 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-cysteine:2-oxoglutarate aminotransferase. Other names in common use include cysteine aminotransferase, L-cysteine aminotransferase, and CGT. This enzyme participates in cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
References
- CHATAGNER F, SAURET-IGNAZI G (June 1956). "[Role of transamination and pyridoxal phosphate in the enzymatic formation of hydrogen sulfide from cysteine by the rat liver under anaerobiosis.]". Bull. Soc. Chim. Biol. 38 (2–3). Paris: 415–28. PMID 13342749.