Protein-disulfide reductase
| protein-disulfide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.1.8 | ||||||||
| CAS no. | 9029-19-0 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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+
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.[1]
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.