Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol.
The reduction of mixed disulphides of some proteins and GSH [Protein(-SSG)n] is accomplished with GSH as a reductant and a thioltransferase from rat liver as a catalyst, thus: See article. The spontaneous reaction is negligible in comparison with the enzymic reaction in vivo, and any direct reduction with glutathione reductase is not detectable with the substrates used. The reduction is only indirectly dependent on NADPH, which is required for the regeneration of GSH from GSSG. Other protein disulphides apparently are reduced via analogous GSH-dependent reactions
D000818:Animals; D003600:Cytosol / Q000201:enzymology*; D004220:Disulfides / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D011506:Proteins / Q000378:metabolism; D051381:Rats; D013466:Sulfurtransferases / Q000378:metabolism*
D004220:Disulfides; D011506:Proteins; D013466:Sulfurtransferases; D005978:Glutathione