Thioltransferase can utilize cysteamine as same as glutathione as a reductant during the restoration of cystamine-treated glucose 6-phosphate dehydrogenase activity.
Glucose 6-phosphate dehydrogenase (G6PD) [EC 1.1.1.49] is inactivated by the incubation with cystamine very efficiently, but not by oxidized glutathione. This inactivation advanced following the incubation-time and concentration of cystamine. The inactivated-G6PD is restored its activity by the treatment of thioltransferase with 1 mM cysteamine or reduced glutathione (GSH) much more effectively than only by thiols. For the first time, we suggested thioltransferase can utilize cysteamine in stead of GSH during its thiol/disulfide exchange reaction activity.
Terada
T
T
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.
D000818:Animals; D003538:Cystamine / Q000378:metabolism / Q000494:pharmacology*; D003543:Cysteamine / Q000378:metabolism / Q000494:pharmacology*; D003545:Cysteine / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004793:Enzyme Reactivators; D005954:Glucosephosphate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D054477:Glutaredoxins; D005978:Glutathione / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D008099:Liver / Q000201:enzymology; D008623:Mercaptoethanol / Q000494:pharmacology; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D011490:Protein Disulfide Reductase (Glutathione); D011817:Rabbits
D004793:Enzyme Reactivators; D054477:Glutaredoxins; D003543:Cysteamine; D008623:Mercaptoethanol; D010088:Oxidoreductases; D005954:Glucosephosphate Dehydrogenase; D011490:Protein Disulfide Reductase (Glutathione); D005978:Glutathione; D003545:Cysteine; D003538:Cystamine; D004229:Dithiothreitol