An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. II. Second site revertants of the thiodigalactoside-dependent proton leak by the Val177/Asn319 permease.

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Article

An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. II. Second site revertants of the thiodigalactoside-dependent proton leak by the Val177/Asn319 permease.

The Journal of biological chemistry - 5 Mar 1991

Eelkema J A, O'Donnell M A, Brooker R J

Abstract excerpt

The double mutant of the lactose permease containing Val177/Asn319 exhibits proton leakiness by two pathways (see Brooker, R. J. (1991) J. Biol Chem. 266, 4131-4138). One type of H+ leakiness involves the uncoupled influx of H+ (leak A pathway) while a second type involves the coupled influx of H...

Topics

Base Sequence
Benzoates
Benzoic Acid
Biological Transport
Cellobiose
Escherichia coli
Escherichia coli Proteins
Galactosides
Hydrogen-Ion Concentration
Lactose
Maltose

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Melibiose

Membrane Potentials

Membrane Transport Proteins

Monosaccharide Transport Proteins

Mutation

Symporters

Thiogalactosides

Source

Open in PubMed

Identifiers

PMID: 1999408

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1999408-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. II. Second site revertants of the thiodigalactoside-dependent proton leak by the Val177/Asn319 permease.PMID 1999408Read ↗

A triple mutant, K319N/H322Q/E325Q, of the lactose permease cotransports H+ with thiodigalactoside.Semantic proximity Read ↗

Characterization of the double mutant, Val-177/Asn-322, of the lactose permease.Semantic proximity Read ↗

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

A suppressor analysis of residues involved in cation transport in the lactose permease: identification of a coupling sensor.Semantic proximity Read ↗

Evidence that the asparagine 322 mutant of the lactose permease transports protons and lactose with a normal stoichiometry and accumulates lactose against a concentration gradient.Semantic proximity Read ↗

Screening of an intragenic second-site suppressor of purine-cytosine permease from Saccharomyces cerevisiae. Possible role of Ser272 in the base translocation process.Semantic proximity Read ↗

An analysis of suppressor mutations suggests that the two halves of the lactose permease function in a symmetrical manner.Semantic proximity Read ↗

Identification of valine 177 as a mutation altering specificity for transport of sugars by the Escherichia coli lactose carrier. Enhanced specificity for sucrose and maltose.Semantic proximity Read ↗

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

Replacement of Lys by Glu in a transmembrane segment strongly impairs the function of the uracil permease from Saccharomyces cerevisiae.Semantic proximity Read ↗

Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli.Semantic proximity Read ↗

Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein.Semantic proximity Read ↗

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