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Article

Characterization of Escherichia coli lactose carrier mutants that transport protons without a cosubstrate. Probes for the energy barrier to uncoupled transport.

The Journal of biological chemistry - 15 Jun 1990

King S C, Wilson T H

Abstract excerpt

The Escherichia coli lactose carrier is an energy-transducing H+/galactoside cotransport protein which strictly couples sugar and proton transport in 1:1 stoichiometry. Here we describe five lactose carrier mutants which catalyze "uncoupled" sugar-independent H+ transport. Symptoms similar to uncoupling by a proton ionophore have been observed in cells expressing these mutant carriers. The mutations occur at two...

Topics

Biological Transport
Cell Membrane
Escherichia coli
Escherichia coli Proteins
Hydrogen-Ion Concentration
Kinetics
Membrane Potentials
Membrane Transport Proteins
Methylgalactosides
Monosaccharide Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protons

Symporters

Thiogalactosides

Valine

Source

Identifiers

PMID: 2161839

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2161839-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Characterization of Escherichia coli lactose carrier mutants that transport protons without a cosubstrate. Probes for the energy barrier to uncoupled transport.PMID 2161839Read ↗

Uncoupling in secondary transport proteins. A mechanistic explanation for mutants of lac permease with an uncoupled phenotype.Semantic proximity Read ↗

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