In enzymology, a protein-disulfide reductase (EC 1.8.1.8) is an enzyme that catalyzes the chemical reaction
protein dithiol + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } protein disulfide + NAD(P)H + H+ Humans have an enzyme of this type which is coded by the gene NXN (nucleoredoxin), and is involved in the regulation of the Wnt signaling pathway. 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.
Structural studies As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1UC7, PDB: 1VRS, PDB: 1Z5Y, PDB: 2FWE, PDB: 2FWF, PDB: 2FWG, PDB: 2FWH, and PDB: 2PPT.
References
HATCH MD, TURNER JF (1960). "A protein disulphide reductase from pea seeds". Biochem. J. 76 (3): 556–62. doi:10.1042/bj0760556. PMC 1204833. PMID 13712218.
