The inhibition by saccharin and cyclamate of phosphotransferase and phosphohydrolase activities of glucose-6-phosphatase
Document Type
Article
Department or Administrative Unit
Chemistry
Publication Date
3-1974
Abstract
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 3.1.3.9). 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.
Recommended Citation
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
Journal
Biochimica et Biophysica Acta (BBA) - Enzymology
Rights
Copyright © 1974 Published by Elsevier B.V.
Comments
This article was originally published in Biochimica et Biophysica Acta (BBA) - Enzymology. The full-text article from the publisher can be found here.
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