Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Physiological studies on regulation of glycerol utilization by the phosphoenolpyruvate:sugar phosphotransferase system in Enterococcus faecalis.

Journal of bacteriology - 1 Dec 1990

Romano A H, Saier M H, Harriott O T, Reizer J

Abstract excerpt

In vitro studies with purified glycerol kinase from Enterococcus faecalis have established that this enzyme is activated by phosphorylation of a histidyl residue in the protein, catalyzed by the phosphoenolpyruvate-dependent phosphotransferase system (PTS), but the physiological significance of this observation is not known. In the present study, the regulation of glycerol uptake was examined in a wild-type...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biological Transport
Share to Enterococcus faecalis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genetic Complementation Test

Share to Glucose

Share to Glycerol

Share to Mutation

Share to Phosphoenolpyruvate Sugar Phosphotransferase System

Share to Phosphorylation

Source

Open in PubMed Open full text

Identifiers

PMID: 2123855
DOI: 10.1128/jb.172.12.6741-6748.1990
PMCID: PMC210788

Genes

PTS

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Physiological studies on regulation of glycerol utilization by the phosphoenolpyruvate:sugar phosphotransferase system in Enterococcus faecalis.PMID 2123855Read ↗

Catabolite control of Escherichia coli regulatory protein BglG activity by antagonistically acting phosphorylations.Semantic proximity Read ↗

Utilisation of glycerol and glycerol 3-phosphate is differently affected by the phosphotransferase system in Bacillus subtilis.Semantic proximity Read ↗

A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo.Semantic proximity Read ↗

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

The glucose permease of the phosphotransferase system of Bacillus subtilis: evidence for IIGlc and IIIGlc domains.Semantic proximity Read ↗

Contribution of the phosphoenolpyruvate:mannose phosphotransferase system to carbon catabolite repression in Lactobacillus pentosus.Semantic proximity Read ↗

Glycerol-3-phosphate-induced catabolite repression in Escherichia coli.Semantic proximity Read ↗

In Vivo Activity of Enzymatic and Regulatory Components of the Phosphoenolpyruvate:Sugar Phosphotransferase System in Mycoplasma pneumoniaeSemantic proximity Read ↗

Analysis of mutations that uncouple transport from phosphorylation in enzyme IIGlc of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system.Semantic proximity Read ↗

Inducer exclusion in Escherichia coli by non-PTS substrates: the role of the PEP to pyruvate ratio in determining the phosphorylation state of enzyme IIAGlc.Semantic proximity Read ↗

Regulatory functions of serine-46-phosphorylated HPr in Lactococcus lactis.Semantic proximity Read ↗

Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.