The sequence of amino acid residues around the oxidation-reduction active disulfide in yeast glutathione reductase.
A 14-residue peptide containing the oxidation-reduction active cystine residue from yeast glutathione reductase has been isolated from proteolytic digests of the enzyme in which the free sulfhydryl groups had been reacted with N-ethylmaleimide. The sequence of this disulfide-containing peptide was found to be:(see article). The sequence was highly homologous with the active cystine regions in Escherichia coli and pig heart lipoamide dehydrogenase. The sequences of three of the postulated four thiol-containing regions of the enzyme are also presented, as well as evidence supporting the view that the enzyme is composed of two identical subunits.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002848:Chromatography, DEAE-Cellulose; D008058:Dihydrolipoamide Dehydrogenase; D004220:Disulfides / Q000032:analysis; D004926:Escherichia coli / Q000201:enzymology; D005033:Ethylmaleimide; D005980:Glutathione Reductase / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis; D011402:Pronase; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013045:Species Specificity; D013552:Swine; D013820:Thermolysin; D014357:Trypsin
D004220:Disulfides; D010446:Peptide Fragments; D008058:Dihydrolipoamide Dehydrogenase; D005980:Glutathione Reductase; D014357:Trypsin; D011402:Pronase; D013820:Thermolysin; D005033:Ethylmaleimide