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Enzymatic catalysis of the reversible sulfitolysis of glutathione disulfide and the biological reduction of thiosulfate esters

, : Enzymatic catalysis of the reversible sulfitolysis of glutathione disulfide and the biological reduction of thiosulfate esters. Archives of Biochemistry and Biophysics 163(1): 283-289

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PMID: 4152871

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Related references

Gilbert, H.F., 1989: Catalysis of thiol/disulfide exchange: single-turnover reduction of protein disulfide-isomerase by glutathione and catalysis of peptide disulfide reduction. Protein disulfide-isomerase, a protein localized to the lumen of the endoplasmic reticulum of eukaryotic cells, catalyzes the posttranslational formation and rearrangement of protein disulfide bonds. As isolated from bovine liver, the enzyme conta...

Eriksson, B., 1966: On the synthesis and enzymatic reduction of the coenzyme A-glutathione mixed disulfide. Acta Chemica Scandinavica 20(4): 1178-1179

Eriksson, S.; Guthenberg, C.; Mannervik, B., 1974: The nature of the enzymatic reduction of the mixed disulfide of coenzyme A and glutathione. Febs Letters 39(3): 296-300

Keire, D.A.; Rabenstein, D.L., 1989: Nmr studies of thiol disulfide chemistry i. kinetics and equilibria of the reduction of captopril disulfide and captopril glutathione mixed disulfide by glutathione. The kinetics and equilibria of the reduction of captopril disulfide (CpSSCp) and captopril-glutathione mixed disulfide (GSSCp) by glutathione (GSH) have been studied by 1H and 13C NMR. Reduction takes place by thiol/disulfide exchange: GSH + CpSSC...

Drescher, D.F.; Follmann, H.; Haeberlein, I., 1998: Sulfitolysis and thioredoxin-dependent reduction reveal the presence of a structural disulfide bridge in spinach chloroplast fructose-1,6-bisphosphatase. A significant difference between cytosolic and chloroplastic fructose-1,6-bisphosphatase (FbPase) is an extra peptide in the middle of chloroplast FbPase which contains three additional cysteine residues. Sit-directed mutagenesis experiments have...

Ruoppolo, M.; Freedman, R.B.; Pucci, P.; Marino, G., 1996: Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase. Protein folding, associated with oxidation and isomerization of disulfide bonds, was studied using reduced and denatured RNase T-1 (rd-RNase T-1) and mixed disulfide between glutathione and reduced RNase T-1 (GS-RNase T-1) as starting materials. F...

Anonymous, 1950: Metabolism of inorganic nitrite and nitrate esters II Enzymatic reduction of nitroglycerine and ervthritol tetranitrate by glutathione

Hwang C J.; Allen K.G.D., 1990: Quantitation of phospholipid hydroperoxide by a coupled glutathione peroxidase and glutathione disulfide specific glutathione reductase assay with prior enzymatic hydrolysis. FASEB Journal 4(3): A663

Schwaller, M.; Wilkinson, B.; Gilbert, H.F., 2002: Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase. Protein-disulfide isomerase (PDI) catalyzes the formation and isomerization of disulfides during oxidative protein folding. This process can be error-prone in its early stages, and any incorrect disulfides that form must be rearranged to their nat...

Janes, W.; Schulz, G.E., 1990: Role of the charged groups of glutathione disulfide in the catalysis of glutathione reductase: crystallographic and kinetic studies with synthetic analogues. Six analogues of glutathione disulfide were synthesized. All of them involved the abolishment of charges, either by amidation of carboxylates or by removal of amino groups. Four of these analogues could be bound to crystalline oxidized glutathione...