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Literature DB >> 2009932

Inhibition of phosphoenolpyruvate carboxykinase by 6-phosphogluconate in rat liver.

Abstract

Various concentrations of 6-phosphogluconate inhibit rat liver phosphoenolpyruvate carboxykinase activity. 0.04 mM 6-phosphogluconate, which is the concentration found in vivo, caused a 50% inhibition of 6-phosphoenolpyruvate carboxykinase activity. 6-Phosphogluconate lowered the Vmax of the enzyme and increased the concentration of phosphoenolpyruvate required to achieve one-half of the maximum velocity. The role of 6-phosphogluconate as a regulator of the coordination of fluxes through three metabolic pathways is discussed.

Entities: Chemical Species

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Year: 1991 PMID： 2009932 DOI： 10.1007/bf01958149

Source DB: PubMed Journal: Experientia ISSN： 0014-4754

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References

17 in total

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Inhibition of phosphoenolpyruvate carboxykinase by 6-phosphogluconate in rat liver.

Review 1. Hormonal regulation of hepatic gluconeogenesis and glycolysis.

2. Apparent unbalance between the activities of 6-phosphogluconate and glucose-6-phosphate dehydrogenases in rat liver.

Review 3. Functional heterogeneity of periportal and perivenous hepatocytes.

4. Fructose 2,6-bisphosphate: a mediator of hormone action at the fructose 6-phosphate/fructose 1,6-bisphosphate substrate cycle.

5. Control of gluconeogenesis and of enzymes of glycogen metabolism in isolated rat hepatocytes. A parallel study of the effect of phenylephrine and of glucagon.

6. Regulation of pyruvate kinase by 6-phosphogluconate in isolated hepatocytes.

7. The zonation of liver and the distribution of fructose 2,6-bisphosphate in rat liver.

8. Regulation of hepatic phosphofructokinase by 6-phosphogluconate.

9. Fructose 2,6-bisphosphate. A new activator of phosphofructokinase.

10. Control of the fructose-6-phosphate/fructose 1,6-bisphosphate cycle in isolated hepatocytes by glucose and glucagon. Role of a low-molecular-weight stimulator of phosphofructokinase.