Suppression of urease levels in Streptococcus salivarius by cysteine, related compounds and by sulfide.

Urease synthesis in Streptococcus salivarius is induced by an acid environment, carbohydrate and a high growth rate. We now report that both cysteine and sulfide above 1 mM strongly suppress S. salivarius urease levels. Close structural relatives of cysteine (cysteamine, ethanedithiol and penicillamine) at 5 mM buffered to pH 7.0 also caused urease suppression, but thiols in general (2-mercaptoethanol, dithiothreitol and glutathione) did not. In cultures buffered below pH 5.9, the cysteine-induced urease suppression was lifted substantially, but the sulfide suppression increased, suggesting involvement of different processes. Urease activity was inhibited 50% by 5 mM mercaptoethanol but unaffected by 5 mM cysteine or sulfide, hence modification of enzyme activity by thiols is not directly related to suppression of their levels in culture. Cysteine, arising primarily through protein hydrolysis which also raises the pH, could be a surrogate pH feedback signal for nearby alkaline conditions, and sulfide may reflect activity of periodontopathic plaques.