Protein-disulfide reductase

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+
protein-disulfide reductase
Identifiers
EC no.1.8.1.8
CAS no.9029-19-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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 1UC7, 1VRS, 1Z5Y, 2FWE, 2FWF, 2FWG, 2FWH, and 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.


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