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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-disulfide reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.8.1.8 | ||||||||
CAS no. | 9029-19-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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.
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.
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