Protein-disulfide reductase (glutathione)

In enzymology, a protein-disulfide reductase (glutathione) (EC 1.8.4.2) is an enzyme that catalyzes the chemical reaction

2 glutathione + protein-disulfide ${\displaystyle \rightleftharpoons }$ glutathione disulfide + protein-dithiol

Thus, the two substrates of this enzyme are glutathione and , whereas its two products are glutathione disulfide and .

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: 1006–11. 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: 68–77. doi:10.1016/0304-4165(74)90336-5.