Cysteine transaminase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 2.6.1.3
- BRENDA references for 2.6.1.3 (Recommended.)
- PubMed references for 2.6.1.3
- PubMed Central references for 2.6.1.3
- Google Scholar references for 2.6.1.3
- CHATAGNER F, SAURET-IGNAZI G (Paris). "[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.: 415–28. PMID 13342749.
[edit] External links
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- The CAS registry number for this enzyme class is 9030-32-4.