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. 1969 Jun;98(3):1109–1113. doi: 10.1128/jb.98.3.1109-1113.1969

Selective Inhibition of Bacterial Enzymes by Free Fatty Acids

John Ferdinandus a,1, J B Clark a
PMCID: PMC315302  PMID: 4306971

Abstract

Octanoic acid inhibits, in vitro, the bacterial enzymes glucose-6-phosphate dehydrogenase, phosphofructokinase, pyruvate kinase, fumarase, lactate dehydrogenase, and the malic enzyme of Arthrobacter crystallopoietes. The free fatty acid appears to act as an inhibitor of lipogenesis, although it does not affect the rate of gluconeogenesis. To demonstrate that this inhibition may be of physiological significance in vivo, those enzymes not involved in lipogenesis, such as fructose-1, 6-diphosphatase, phosphoglucomutase, phosphohexoisomerase, aconitase, nicotinamide adenine dinucleotide phosphate (NADP) isocitrate dehydrogenase, NADP glutamate dehydrogenase, malate dehydrogenase, and isocitrate lyase, were assayed and found not to be inhibited by the free fatty acid.

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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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