Abstract
PHOSPHORYLATION of glucose, the hexokinase reaction, is an irreversible one which, however, is reversible by a specific phosphatase, the glucose-6-phosphatase (G-6-pase). Therefore the velocity of the phosphorylation of glucose is not only dependent on the activity of the hexokinase, but is also a result of the contrary action of both the enzymes. It was shown by some authors1,2 that the activity of G-6-pase is different in varying conditions of metabolism. Tissues or cells with a high catabolism of carbohydrates show a significantly decreased activity of G-6-pase, besides an increased activity of hexokinase2. Highly glycolysing tumours represent tissues with a remarkable catabolism of carbohydrates and also show a decreased activity of G-6-pase3,4. Hitherto no tumour has been found with a noticeable activity of this enzyme. On the other hand, it will be expected that tissues with a diminished consumption of glucose or increased synthesis of glucose from non-carbohydrate sources via the Embden–Meyerhof pathway exhibit an enhanced activity of G-6-pase. Accordingly Mokrasch1 found increased activity of phosphatase in diabetic liver.
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HEISE, E., GÖRLICH, M. Proteolytic Activation of Glucose-6-phosphatase in Normal, Diabetic and Hepatomic Rat Livers. Nature 197, 1311–1312 (1963). https://doi.org/10.1038/1971311a0
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DOI: https://doi.org/10.1038/1971311a0
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