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PMID: 2177909 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The lac permease of Escherichia coli: site-directed mutagenesis studies on the mechanism of beta-galactoside/H+ symport.

Research in microbiology ·Vol. 141 ·No. 3 ·1990-00-00 ·Pages 290-308

Roepe PD, Consler TG, Menezes ME, Kaback HR

Abstract

In this communication, we summarize site-directed mutagenesis studies of the lac permease from Escherichia coli, a prototypic H(+)-coupled active transport protein. We classify mutant permeases by phenotype, and suggest possible roles for some individual residues in the mechanism of H+/lactose symport. Although high-resolution structural information is not presently available, kinetic analysis of the partial reactions catalysed by the mutant permeases, as well as biophysical studies, suggest an evolving model for the mechanism of H+/lactose symport.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/genetics,metabolism Binding Sites Biological Transport, Active Escherichia coli/enzymology,genetics Escherichia coli Proteins Lactose/metabolism Membrane Proteins/genetics,metabolism Membrane Transport Proteins/genetics,metabolism Models, Molecular Molecular Sequence Data Monosaccharide Transport Proteins Mutagenesis, Site-Directed Proline Protein Conformation Protons Symporters Tryptophan Tyrosine
Chemicals
Bacterial Proteins Escherichia coli Proteins LacY protein, E coli Membrane Proteins Membrane Transport Proteins Monosaccharide Transport Proteins Protons Symporters Tyrosine Tryptophan lactose permease Proline Lactose
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Roepe P D
Department of Physiology, Howard Hughes Medical Institute, University of California, Los Angeles 90024-1570.
Consler T G
Menezes M E
Kaback H R
Article Info
Journal
Research in microbiology
Abbr.
Res Microbiol
ISSN
0923-2508
Published
1990-00-00
Pages
290-308
Language
English
Region
France
NLM ID
8907468
Subset
IM
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