can inhibit enolase activity in biological contexts, such as cells and animal tissues. Methylglyoxal has also been described as an inhibitor of human enolase. Active site transition state analogue Enolase inhibitors have been explored pre-clinically for the treatment of various microbial pathogens, as well as in precision oncology for tumors with 1p36 homozygous deletions, that lack ENO1. Fluoride is a known competitor of enolase's substrate 2-PG. Fluoride can a complex with magnesium and phosphate, which binds in the active site instead of 2-PG. One study found that fluoride could inhibit bacterial enolase in vitro. The Enolase inhibitory activity of Fluoride anion may contribute to the anti-cavity effect of fluoride toothpaste, by limiting lactic acid (a product of glycolysis, which requires Enolase) production. References Further reading Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 471-494. External links Moonlighting proteins Glycolysis enzymes Glycolysis