Protein-disulfide reductase
From Wikipedia, the free encyclopedia
In enzymology, a protein-disulfide reductase (EC 1.8.1.8) is an enzyme that catalyzes the chemical reaction
- protein dithiol + NAD(P)+
protein disulfide + NAD(P)H + H+
The 3 substrates of this enzyme are protein dithiol, NAD+, and NADP+, whereas its 4 products are protein disulfide, NADH, NADPH, 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 protein-dithiol:NAD(P)+ oxidoreductase. Other names in common use include protein disulphide reductase, insulin-glutathione transhydrogenase, disulfide reductase, and NAD(P)H2:protein-disulfide oxidoreductase.
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[edit] Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1UC7, 1VRS, 1Z5Y, 2FWE, 2FWF, 2FWG, 2FWH, and 2PPT.
[edit] References
- IUBMB entry for 1.8.1.8
- BRENDA references for 1.8.1.8 (Recommended.)
- PubMed references for 1.8.1.8
- PubMed Central references for 1.8.1.8
- Google Scholar references for 1.8.1.8
- HATCH MD, TURNER JF (1960). "A protein disulphide reductase from pea seeds". Biochem. J. 76: 556–62. PMID 13712218.
[edit] External links
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- The CAS registry number for this enzyme class is 9029-19-0.

