Regulation of glycerol and maltose uptake by the IIAGlc-like domain of IINag of the phosphotransferase system in Salmonella typhimurium LT2.

doi:10.1007/BF02190806

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Article

Regulation of glycerol and maltose uptake by the IIAGlc-like domain of IINag of the phosphotransferase system in Salmonella typhimurium LT2.

Molecular & general genetics : MGG - 28 Jul 1995

van der Vlag J, Postma P W

Abstract excerpt

In Enterobacteriaceae the nonphosphorylated form of IIAGlc of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) can inhibit the uptake and subsequent metabolism of glycerol and maltose by binding to, and inhibiting, glycerol kinase and the MalK protein of the maltose transport sys...

Topics

Acetylglucosamine
Adenylyl Cyclases
Amino Acid Sequence
Biological Transport
Deoxyglucose
Escherichia coli Proteins
Glycerol
Glycerol Kinase
Maltose
Membrane Transport Proteins
Methylglucosides
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Monosaccharide Transport Proteins

Mutation

Phosphoenolpyruvate Sugar Phosphotransferase System

Salmonella typhimurium

Sequence Alignment

Symporters

Source

Open in PubMed

Identifiers

PMID: 7651347
DOI: 10.1007/BF02190806

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7651347-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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