Phospho-beta-glucosidases and beta-glucoside permeases in Streptococcus, Bacillus, and Staphylococcus.
The presence of phospho-beta-glucosidases and beta-glucoside permeases was found in strains of Streptococcus, Bacillus, and Staphylococcus. In streptococci, the phospho-beta-glucosidase activity depends on the antigenic group. The highest activity was found in strains of group D. In group D strains, phospho-beta-glucosidase activity is induced by beta-methyl glucoside and cellobiose but not by thiophenyl beta-glucoside (TPG). With the exception of four strains isolated in Japan, all strains of B. subtilis tested possess an inducible phospho-beta-glucosidase activity, beta-methyl glucoside, cellobiose, and TPG acting as inducers. S. aureus strains possess phospho-beta-glucosidase A but not phospho-beta-glucosidase B, whereas most S. albus strains show no detectable phospho-beta-glucosidase activity. The prompt fermentation of beta-methyl glucoside by S. aureus strains could serve as an additional criterion for their differentiation from S. albus. A comparative investigation of the active uptake of (14)C-TPG showed that a Streptococcus group D strain and a B. subtilis strain posses two inducible permeases with characteristics similar to the beta-glucoside permeases I and II of Enterobacteriaceae. In S. aureus, TPG is accumulated by a constitutive permease with high affinity for aromatic beta-glucosides and glucose. The active uptake of TPG by S. aureus appears to depend on the activity of the phosphoenol pyruvate-dependent phosphotransferase system.
D001407:Bacillus / Q000201:enzymology*; D001431:Bacteriological Techniques; D002247:Carbon Isotopes; D004790:Enzyme Induction; D005959:Glucosidases; D006027:Glycosides / Q000378:metabolism / Q000494:pharmacology; D026901:Membrane Transport Proteins; D012703:Serotyping; D013210:Staphylococcus / Q000201:enzymology*; D013291:Streptococcus / Q000201:enzymology*
D002247:Carbon Isotopes; D006027:Glycosides; D026901:Membrane Transport Proteins; D005959:Glucosidases