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Isolation, characterization and nucleotide sequence of the Streptococcus mutans lactose-specific Enzyme II (lacE) gene of the PTS and the phospho- -galactosidase (lacG) gene
Author(s) -
Allen L. Honeyman,
Roy Curtiss
Publication year - 1993
Publication title -
journal of general microbiology/journal of general microbiology
Language(s) - English
Resource type - Journals
eISSN - 2059-9323
pISSN - 0022-1287
DOI - 10.1099/00221287-139-11-2685
Subject(s) - streptococcus mutans , lactococcus lactis , gene , lactose , operon , biochemistry , lactobacillus casei , biology , pep group translocation , lactose permease , nucleotide , homology (biology) , microbiology and biotechnology , streptococcus gordonii , nucleic acid sequence , chemistry , phosphoenolpyruvate carboxykinase , genetics , escherichia coli , bacteria , streptococcaceae , permease , lactic acid , antibiotics , fermentation
The lacE and lacG genes from Streptococcus mutans have been isolated and characterized, and their nucleotide sequence has been determined. The lacE gene encodes the lactose-specific Enzyme II component of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The lacG gene encodes the phospho-beta-galactosidase which cleaves the lactose phosphate that is formed by the lactose PTS. The S. mutans lacE and lacG genes are located in the same operon as the tagatose genes. S. mutans metabolizes lactose via the tagatose phosphate pathway. The deduced LacE and LacG proteins of S. mutans display high homology with the corresponding proteins from Lactococcus lactis, Staphylococcus aureus and Lactobacillus casei.

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