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Science 9 December 1966:
Vol. 154. no. 3754, pp. 1357 - 1360
DOI: 10.1126/science.154.3754.1357
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Articles

Feedback Inhibition of Key Glycolytic Enzymes in Liver: Action of Free Fatty Acids

George Weber 1, Hazel J. Hird Convery 1, Michael A. Lea 1, and Nancy B. Stamm 1

1 Department of Pharmacology, Indiana University School of Medicine, Indianapolis 46207

Increasing concentrations of sodium octanoate were progressively inhibitory to the activities of glucokinase, hexokinase, phosphofructokinase, and pyruvate kinase. Glucose-6-phosphate and 6-phosphogluconate dehydrogenases were also markedly inhibited. Other enzymes of carbohydrate metabolism such as lactate dehydrogenase, phosphohexose isomerase, and fructose-1,6-diphosphatase were not decreased. Among the key glycolytic enzymes, the inhibition of pyruvate kinase by the fatty acid was most marked. The biological significance of the inhibition of the key glycolytic enzymes is interpreted as a feedback inhibitory mechanism in regulation of fatty acid biosynthesis. The mechanism may function for rapid adaptation by which the organism can use the fatty acid level as a metabolic directional switch in decreasing glycolysis and turning on gluconeogenesis.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Defective Fatty Acid-mediated beta-Cell Compensation in Zucker Diabetic Fatty Rats.
H. Hirose, Y. H. Lee, L. R. Inman, Y. Nagasawa, J. H. Johnson, and R. H. Unger (1996)
J. Biol. Chem. 271, 5633-5637
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Skeletal Muscle: Basic and Clinical Aspects and Illustrative New Diseases.
C. M. PEARSON, R. F. COLEMAN, W. M. FOWLER JR., W. F. H. M. MOMMAERTS, T. L. MUNSAT, and J. B. PETER (1967)
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