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Article

Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli.

The Journal of biological chemistry - 11 Mar 1994

Franco P J, Brooker R J

Abstract excerpt

Acidic residues which are found on transmembrane segments within the lactose permease may play an important role in H+ and/or sugar recognition. To examine the functional roles of Glu-269 and Glu-325, we have constructed a variety of amino acid substitutions (e.g. aspartate, glycine, alanine, serine, or glutamine) via site-directed mutagenesis. At position 269, all mutations appear to have a detrimental effect on...

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PMID: 7907327

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Research trail→

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Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli.PMID 7907327Read ↗

Physiological evidence for an interaction between helices II and XI in the melibiose carrier of Escherichia coli.Semantic proximity Read ↗

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

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

Lysine 319 interacts with both glutamic acid 269 and aspartic acid 240 in the lactose carrier of Escherichia coli.Semantic proximity Read ↗

Physiological evidence for an interaction between helix XI and helices I, II, and V in the melibiose carrier of Escherichia coli.Semantic proximity Read ↗

Identification and characterization of functional residues in a Na+/H+ antiporter (NhaA) from Escherichia coli by random mutagenesis.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 ↗

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

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.Semantic proximity Read ↗

The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease.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 ↗

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