Open AccessQuasi‐irreversible inhibition of enolase of Streptococcus mutans by flouride
Author(s) -
Curran Timothy M.,
Buckley Daniel H.,
Marquis Robert E.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06902.x
Subject(s) - enolase , fluoride , streptococcus mutans , phosphoenolpyruvate carboxykinase , chemistry , biochemistry , yeast , intracellular , sodium fluoride , enzyme , microbiology and biotechnology , bacteria , biology , inorganic chemistry , genetics , immunohistochemistry , immunology
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 Al 3+ or Be 2+ 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.