Feedback inhibition of key glycolytic enzymes in liver: Action of free fatty acids

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

Research output: Contribution to journalArticlepeer-review

86 Scopus citations


Increasing concentrations of sodium octanoate were progressively inhibitory to the activities pf 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.

Original languageEnglish (US)
Pages (from-to)1357-1360
Number of pages4
Issue number3754
StatePublished - 1966
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General


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