Protein-disulfide reductase (glutathione)
| protein-disulfide reductase (glutathione) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.8.4.2 | ||||||||
| CAS number | 9082-53-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a protein-disulfide reductase (glutathione) (EC 1.8.4.2) is an enzyme that catalyzes the chemical reaction
- 2 glutathione + protein-disulfide glutathione disulfide + protein-dithiol
Thus, the two substrates of this enzyme are glutathione and protein disulfide, whereas its two products are glutathione disulfide and protein dithiol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:protein-disulfide oxidoreductase. Other names in common use include glutathione-insulin transhydrogenase, insulin reductase, reductase, protein disulfide (glutathione), protein disulfide transhydrogenase, glutathione-protein disulfide oxidoreductase, protein disulfide reductase (glutathione), GSH-insulin transhydrogenase, protein-disulfide interchange enzyme, protein-disulfide isomerase/oxidoreductase, thiol:protein-disulfide oxidoreductase, and thiol-protein disulphide oxidoreductase. This enzyme participates in glutathione metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2IJY.
References
- KATZEN HM, TIETZE F, STETTEN D (1963). "Further studies on the properties of hepatic glutathione-insulin transhydro-genase". J. Biol. Chem. 238: 1006&ndash, 11. PMID 14031343.
- Kohnert KD, Hahn HJ, Zuhlke H, Schmidt S, Fiedler H (1974). "Breakdown of exogenous insulin by Langerhans islets of the pancreas in vitro". Biochim. Biophys. Acta. 338: 68&ndash, 77. doi:10.1016/0304-4165(74)90336-5.