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. 1973 May;114(2):723–728. doi: 10.1128/jb.114.2.723-728.1973

Membrane Translocation of Mannitol in Escherichia coli Without Phosphorylation

Ellen Solomon a,1, Kenji Miyai a,2, E C C Lin a
PMCID: PMC251832  PMID: 4574698

Abstract

Galactosyl-mannitol can be transported into cells of Escherichia coli by β-galactoside permease and can be hydrolyzed rapidly to mannitol and galactose by β-galactosidase. When a mutant strain lacking enzyme I of the phosphoenolpyruvate phosphotransferase system and constitutive in the lactose system was presented with galactosyl-mannitol in which the mannitol moiety was labeled with 3H, the liberated mannitol remained inside the cell if the Enzyme II complex of the phosphoenolpyruvate phosphotransferase system for mannitol was uninduced. It is postualted that one of the enzyme II proteins can still catalyze translocation of mannitol across the cell membrane even when phsophorylation is not possible.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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