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Pathways for lactose/galactose catabolism by Streptococcus salivarius
Author(s) -
Chen YiYwan M,
Betzenhauser Matthew J,
Snyder Jennifer A,
Burne Robert A
Publication year - 2002
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.1574-6968.2002.tb11112.x
Subject(s) - streptococcus salivarius , lactose , galactokinase , galactose , pep group translocation , catabolism , biochemistry , beta galactosidase , microbiology and biotechnology , chemistry , bacteria , biology , enzyme , phosphoenolpyruvate carboxykinase , streptococcus , escherichia coli , gene , genetics
Galactokinase and β‐galactosidase‐deficient strains of Streptococcus salivarius were constructed to define the pathways for lactose and galactose catabolism. It was found that S. salivarius does not possess a lactose‐specific phosphoenolpyruvate phosphotransferase system (PTS), that intracellular lactose was hydrolyzed by β‐galactosidase, and that galactose is catabolized exclusively through the Leloir pathway. The lack of a high‐affinity PTS for lactose may reflect the higher availability of the substrates to soft tissue organisms, such as S. salivarius , compared to dental plaque bacteria.

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