PMID:11785976

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Citation

Núñez, MF, Kwon, O, Wilson, TH, Aguilar, J, Baldoma, L and Lin, EC (2002) Transport of L-Lactate, D-Lactate, and glycolate by the LldP and GlcA membrane carriers of Escherichia coli. Biochem. Biophys. Res. Commun. 290:824-9

Abstract

To examine the substrate specificity of the membrane transport carriers LldP (L-lactate permease) and GlcA (glycolate permease) of Escherichia coli, a mutant strain lacking their structural genes and blocked in the metabolism of the tested substrates was constructed and transformed with a plasmid bearing either the lldP or the glcA gene. Each transformant acquired the ability to accumulate L-lactate, D-lactate, and glycolate against a high concentration gradient. Substrate accumulation was inhibited by carbonyl cyanide m-chlorophenylhydrazone, a hydrophobic proton conductor that dissipates proton motive force. Competition of (14)C-L-lactate transport by nonradioactive L-lactate, D-lactate, and glycolate in LldP synthesizing cells and competition of (14)C-glycolate transport by the same three substrates in GlcA synthesizing cells showed that both carriers effectively transported all three substrates with a K(i) value ranging from 10 to 20 microM. D-Lactate does not appear to have a permease of its own. Utilization of the compound depends mainly on LldP.

Links

PubMed Online version:10.1006/bbrc.2001.6255

Keywords

Acetic Acid/pharmacology; Binding, Competitive/drug effects; Biological Transport, Active/drug effects; Biological Transport, Active/physiology; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Glycolates/metabolism; Glycolates/pharmacokinetics; Lactic Acid/metabolism; Lactic Acid/pharmacokinetics; Membrane Transport Proteins/genetics; Membrane Transport Proteins/metabolism; Protons; Stereoisomerism; Substrate Specificity; Transformation, Bacterial/genetics

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