Quasi-irreversible inhibition of enolase of Streptococcus mutans by fluoride

• Published in: FEMS microbiology letters Vol. 119; no. 3; p. 283
• Main Authors: Curran, T M, Buckley, D H, Marquis, R E
• Format: Journal Article
• Language: English
• Published: England 15-06-1994
• Subjects: Fluorides - pharmacology; Glycolysis - drug effects; Hydrogen-Ion Concentration; Phosphoenolpyruvate - metabolism; Phosphopyruvate Hydratase - antagonists & inhibitors; Phosphopyruvate Hydratase - metabolism; Streptococcus mutans - drug effects; Streptococcus mutans - enzymology; Yeasts
• ISSN: 0378-1097

Fluoride at concentrations greater than 0.01 mM was found to be a quasi-irreversible inhibitor of enolase of permeabilized cells of Streptococcus mutans GS-5 and also of isolated yeast enolase. The inhibition appeared to be of the type that has been described for P-ATPases, but was not dependent on added Al3+ or Be2+ ions. Fluoride inhibition of enolase was not reversed by repeatedly washing the permeabilized cells in chilled fluoride-free medium but could be reversed by the product, phosphoenolpyruvate, or by very high levels of the substrate, 2-phosphoglycerate. Irreversible inhibition of glycolysis was not evident after fluoride treatment of intact cells, washing to remove unbound or loosely bound fluoride and addition of glucose, presumably because intracellular levels of phosphoenolpyruvate were sufficiently high to preclude irreversible fluoride inhibition of enolase.