Cysteine transaminase
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. "[Role of transamination and pyridoxal phosphate in the enzymatic formation of hydrogen sulfide from cysteine by the rat liver under anaerobiosis.]". Bull. Soc. Chim. (Paris). Biol. (2–3): 415–28. PMID 13342749.
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|