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Gene Review:

lacE - PTS system lactose-specific IIBC component

Staphylococcus aureus RF122

Alpert, C.A. et al., Breidt, F. et al., Honeyman, A.L. et al., de Vos, W.M. et al., Finkeldei, U. et al., et al.

Alpert, Siebers,

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Disease relevance of lacE

The identity of lacE as encoding Enzyme IIlac was based upon immunoreactivity of the cloned gene product with antibodies raised against purified Enzyme IIlac from S. aureus and an assay of biological function of the protein expressed in Escherichia coli [1].
The gene coding for the lactose-specific Enzyme II of the Lactobacillus casei phosphoenolpyruvate-dependent phosphotransferase system, lacE, has been isolated by molecular cloning and expressed in Escherichia coli [2].
The plasmid-encoded lactose genes of the Lactococcus lactis phosphotransferase system encoding Enzyme IIIlac (lacF) and Enzyme IIlac (lacE) have been identified and cloned in Escherichia coli and L. lactis [3].
The nucleotide and deduced amino acid sequences of the lacE and lacF genes, which code for the lactose-specific Enzyme II and Enzyme III of the Staphylococcus aureus phosphotransferase system, are presented [1].
The complete nucleotide sequences of lacRABCDF and partial nucleotide sequence of lacE from the lactose operon of Streptococcus mutans are presented [4].

High impact information on lacE

Molecular cloning and DNA sequence of lacE, the gene encoding the lactose-specific enzyme II of the phosphotransferase system of Lactobacillus casei. Evidence that a cysteine residue is essential for sugar phosphorylation [2].
The identity of the lacE product as the Enzyme IIlacL.casei was demonstrated by in vitro lactose phosphorylation assays using the protein expressed in E. coli [2].
An open reading frame of 293 codons, designated lacT, was identified upstream of lacE [5].
Isolation, characterization and nucleotide sequence of the Streptococcus mutans lactose-specific enzyme II (lacE) gene of the PTS and the phospho-beta-galactosidase (lacG) gene [6].
The S. mutans lacE and lacG genes are located in the same operon as the tagatose genes [6].

Biological context of lacE

The DNA sequence of the lacE gene and the deduced amino acid sequence are presented [2].

Associations of lacE with chemical compounds

Staphylococcal lactose phosphoenolpyruvate-dependent phosphotransferase system: site-specific mutagenesis on the lacE gene gives evidence that a cysteine residue is responsible for phosphorylation [7].

References

Identification of the genes for the lactose-specific components of the phosphotransferase system in the lac operon of Staphylococcus aureus. Breidt, F., Hengstenberg, W., Finkeldei, U., Stewart, G.C. J. Biol. Chem. (1987) [Pubmed]
Molecular cloning and DNA sequence of lacE, the gene encoding the lactose-specific enzyme II of the phosphotransferase system of Lactobacillus casei. Evidence that a cysteine residue is essential for sugar phosphorylation. Alpert, C.A., Chassy, B.M. J. Biol. Chem. (1990) [Pubmed]
Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis. de Vos, W.M., Boerrigter, I., van Rooyen, R.J., Reiche, B., Hengstenberg, W. J. Biol. Chem. (1990) [Pubmed]
Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans. Rosey, E.L., Stewart, G.C. J. Bacteriol. (1992) [Pubmed]
The lac operon of Lactobacillus casei contains lacT, a gene coding for a protein of the Bg1G family of transcriptional antiterminators. Alpert, C.A., Siebers, U. J. Bacteriol. (1997) [Pubmed]
Isolation, characterization and nucleotide sequence of the Streptococcus mutans lactose-specific enzyme II (lacE) gene of the PTS and the phospho-beta-galactosidase (lacG) gene. Honeyman, A.L., Curtiss, R. J. Gen. Microbiol. (1993) [Pubmed]
Staphylococcal lactose phosphoenolpyruvate-dependent phosphotransferase system: site-specific mutagenesis on the lacE gene gives evidence that a cysteine residue is responsible for phosphorylation. Finkeldei, U., Hengstenberg, W. Protein Eng. (1991) [Pubmed]

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