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. 1967 Mar;102(3):753–759. doi: 10.1042/bj1020753

Inhibition of glucose phosphate isomerase by metabolic intermediates of fructose

J Zalitis 1,*, I T Oliver 1
PMCID: PMC1270324  PMID: 16742490

Abstract

1. Purified rabbit-muscle and -liver glucose phosphate isomerase, free of contaminating enzyme activities that could interfere with the assay procedures, were tested for inhibition by fructose, fructose 1-phosphate and fructose 1,6-diphosphate. 2. Fructose 1-phosphate and fructose 1,6-diphosphate are both competitive with fructose 6-phosphate in the enzymic reaction, the apparent Ki values being 1·37×10−3−1·67×10−3m for fructose 1-phosphate and 7·2×10−3−7·9×10−3m for fructose 1,6-diphosphate; fructose and inorganic phosphate were without effect. 3. The apparent Km values for both liver and muscle enzymes at pH7·4 and 30° were 1·11×10−4−1·29×10−4m for fructose 6-phosphate, determined under the conditions in this paper. 4. In the reverse reaction, fructose, fructose 1-phosphate and fructose 1,6-diphosphate did not significantly inhibit the conversion of glucose 6-phosphate into fructose 6-phosphate. 5. The apparent Km values for glucose 6-phosphate were in the range 5·6×10−4−8·5×10−4m. 6. The competitive inhibition of hepatic glucose phosphate isomerase by fructose 1-phosphate is discussed in relation to the mechanism of fructose-induced hypoglycaemia in hereditary fructose intolerance.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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