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. 1970 Aug;66(4):1190–1198. doi: 10.1073/pnas.66.4.1190

β-GALACTOSIDE TRANSPORT IN BACTERIAL MEMBRANE PREPARATIONS: ENERGY COUPLING VIA MEMBRANE-BOUND D-LACTIC DEHYDROGENASE

Eugene M Barnes Jr 1,*, H R Kaback 1,†
PMCID: PMC335805  PMID: 4394455

Abstract

The transport of β-galactosides by isolated membrane preparations from Escherichia coli strains containing a functional y gene is markedly stimulated by the conversion of D-lactate to pyruvate. The addition of D-lactate to these membrane preparations produces a 19-fold increase in the initial rate of uptake and a 10-fold stimulation of the steady-state level of intramembranal lactose or thiomethylgalactoside. Succinate, DL-α-hydroxybutyrate, and L-lactate partially replace D-lactate, but are much less effective; ATP and P-enolpyruvate, in addition to a number of other metabolites and cofactors, do not stimulate lactose transport by the vesicles. Lactose uptake by the membrane preparations in the presence of D-lactate requires oxygen, and is blocked by electron transport inhibitors and proton conductors; however, uptake is not significantly inhibited by high concentrations of arsenate or oligomycin. Furthermore, the P-enolpyruvate-P-transferase system is not involved in β-galactoside transport by the E. coli membrane vesicles. The findings indicate that the β-galactoside uptake system is coupled to the membrane-bound D-lactic dehydrogenase via an electron transport chain but does not involve oxidative phosphorylation.

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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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