Effect of thioltransferase on the cystamine-activated fructose 1,6-bisphosphatase by its redox regulation.
Fructose 1,6-bisphosphatase [EC. 3.1.3.11] is activated by the treatment with 0.1 mM cystamine up to about 400% compared to its original activity (dithiothreitol-reduced form). Thiol compounds (0.1 mM of cysteamine and dithiothreitol) can restore its activity effectively. Reduced glutathione, at 0.2 mM, also restores fructose 1,6-bisphosphatase activity only in the presence of cystamine. When excess cystamine is removed, the addition of 1.0 U/ml thioltransferase is able to restore FBPase activity very efficiently coexistence with 0.2 mM reduced glutathione though reduced glutathione alone does not work.
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.
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Terada
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Hara
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Yazawa
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Mizoguchi
D000818:Animals; D003538:Cystamine / Q000494:pharmacology*; D004789:Enzyme Activation; D006597:Fructose-Bisphosphatase / Q000187:drug effects* / Q000378:metabolism*; D054477:Glutaredoxins; D005978:Glutathione / Q000378:metabolism / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000494:pharmacology*; D011490:Protein Disulfide Reductase (Glutathione); D011817:Rabbits; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D054477:Glutaredoxins; D013438:Sulfhydryl Compounds; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione); D006597:Fructose-Bisphosphatase; D005978:Glutathione; D003538:Cystamine