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.
Terada
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T
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Hara
T
T
Yazawa
H
H
Mizoguchi
T
T
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