Specificity for the glucose-6-P inhibition site of hexokinase |
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Authors: | I A Rose J V Warms D P Kosow |
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Institution: | The Institute for Cancer Research, Fox Chase Center for Cancer and Medical Sciences, Philadelphia, Pennsylvania 19111 U.S.A. |
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Abstract: | Inhibition of the three animal hexokinase isozymes by the following glucose-6-P analogs has been determined: α-glucose-1,6-P2, α- and β-methyl glucose-6-P, α- and β-glucose-6-P, 2-Cl- and 4F-glucose-6-P, 5-deoxyglucose-6-P, glucose-6-sulfate, and δ-gluconolactone-6-P. Although both anomers of glucose-6-P were about equally active inhibitors, the β-methyl derivative was inactive. Generally the α-methyl and α-PO3? derivatives were good inhibitors though weaker than glucose-6-P except in the case of hexokinase II for which α-glucose-1,6-P2 was an excellent inhibitor. |
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