Cystine reductase
From Wikipedia, the free encyclopedia
In enzymology, a cystine reductase (EC 1.8.1.6) is an enzyme that catalyzes the chemical reaction
- 2 L-cysteine + NAD+ L-cystine + NADH + H+
Thus, the two substrates of this enzyme are L-cysteine and NAD+, whereas its 3 products are L-cystine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-cysteine:NAD+ oxidoreductase. Other names in common use include cystine reductase (NADH), NADH-dependent cystine reductase, cystine reductase (NADH2), and NADH2:L-cystine oxidoreductase. This enzyme participates in cysteine metabolism.
[edit] References
- IUBMB entry for 1.8.1.6
- BRENDA references for 1.8.1.6 (Recommended.)
- PubMed references for 1.8.1.6
- PubMed Central references for 1.8.1.6
- Google Scholar references for 1.8.1.6
- ROMANO AH, NICKERSON WJ (1954). "Cystine reductase of pea seeds and yeasts". J. Biol. Chem. 208: 409–16. PMID 13174550.
- Carroll JE, Kosicki GW, Thibert RJ (1970). "Alpha-substituted cystines as possible substrates for cystine reductase and L-amino acid oxidase". Biochim. Biophys. Acta. 198: 601–3. PMID 5436160.
- Maresca B, Jacobson E, Medoff G, Kobayashi G (1978). "Cystine reductase in the dimorphic fungus Histoplasma capsulatum". J. Bacteriol. 135: 987–92. PMID 211119.
[edit] External links
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- The CAS registry number for this enzyme class is 9029-18-9.