Disease relevance of galP

• The recombinant gene was overexpressed from the E. coli galP promoter, and ProP-(His)6 was shown to be functionally equivalent to wild-type ProP by enzymatic assay of whole cells [1].

High impact information on galP

• All the protein/peptide mass and sequence determinations were in accord with the predictions of amino acid sequence deduced from the DNA sequence of the galP gene [2].
• The capacity of GalP to transport galactose was demonstrated by using galP disruption mutant strains of L. lactis MG1363 [3].
• Recruitment of native E. coli galP-encoded galactose permease for glucose transport required 60 h to synthesize 3-dehydroshikimic acid (60 g/L) and shikimate pathway byproducts in a total yield of 43% (mol/mol) [4].
• The promoter region of the chromosomal galactose permease gene galP of VH32 was replaced by the strong trc promoter [5].
• TUQ2 increased the generation time to approximately 4 h and gave a higher final cell density of 0.5 g/l by expression of galP [6].

Chemical compound and disease context of galP

• Strains of Escherichia coli devoid of systems for the active transport of galactose (galP mgl) still grow on galactose but at rates that are a function of the galactose concentration of the medium: half-maximal growth rates require more than 2 mM-galactose to be present [7].

References