Lipid dependencies, biogenesis and cytoplasmic micellar forms of integral membrane sugar transport proteins of the bacterial phosphotransferase system
Author:
Affiliation:
1. Department of Microbiology and Immunology, Faculty of Pharmacy, Ain Shams University, Abbasia, Cairo, Egypt
2. Department of Molecular Biology, University of California at San Diego, La Jolla, CA 92093-0116, USA
Publisher
Microbiology Society
Subject
Microbiology
Reference83 articles.
1. Dependency of sugar transport and phosphorylation by the phosphoenolpyruvate-dependent phosphotransferase system on membranous phosphatidyl glycerol in Escherichia coli: Studies with a pgsA mutant lacking phosphatidyl glycerophosphate synthase
2. Soluble sugar permeases of the phosphotransferase system in Escherichia coli: evidence for two physically distinct forms of the proteins in vivo
3. Characterization of Soluble Enzyme II Complexes of the Escherichia coli Phosphotransferase System
4. In vitro Interconversion of the Soluble and Membrane- Integrated Forms of the Escherichia coli Glucose Enzyme II of the Phosphoenolpyruvate-Dependent Sugar-Transporting Phosphotransferase System
5. Characterization of theE. coli glucose permease fused to the maltose-binding protein
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