The inhibition by saccharin and cyclamate of phosphotransferase and phosphohydrolase activities of glucose-6-phosphatase
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Saccharin and cyclamate were found to inhibit the glucose-6-phosphate phosphohydrolase and PPi-glucose phosphotransferase activities of beef liver microsomal glucose-6-phosphatase (D-glucose-6-phosphate phosphohydrolase, EC 184.108.40.206). The extent of inhibition decreased with increasing pH in the range pH 4–8. At pH 5.6 inhibition by both compounds was competitive with respect to phosphate substrates and non-competitive with respect to glucose Ki values for saccharin and cyclamate were, respectively, 6.5 and 26 mM for the phosphohydrolase reaction, and were 16 and 68 mM with respect to PPi and 110 and 190 mM with respect to glucose for the phosphotransferase reaction. Of a variety of structural analogs of saccharin and cyclamate, saccharin was the most effective inhibitor tested.
Lygre, D. G. (1974). The inhibition by saccharin and cyclamate of phosphotransferase and phosphohydrolase activities of glucose-6-phosphatase. Biochimica et Biophysica Acta (BBA) - Enzymology, 341(1), 291–297. https://doi.org/10.1016/0005-2744(74)90090-4
Biochimica et Biophysica Acta (BBA) - Enzymology
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