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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...

Topics

Biological Transport
Enterococcus faecalis
Genetic Complementation Test
Glucose
Glycerol
Glycerol Kinase
Mutation
Phosphoenolpyruvate Sugar Phosphotransferase System
Phosphorylation

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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 29 Aug 2026. Prepared record publication-2123855-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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

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