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

Uncoupling of choline-O-sulphate utilization from osmoprotection in Pseudomonas putida.

Molecular microbiology - 1 Dec 2006

Galvão Teca Calcagno, de Lorenzo Victor, Cánovas David

Abstract excerpt

The genomic context of the recognized bet genes for choline-O-sulphate (COS) utilization in Pseudomonas putida KT2440 is such that betC (choline sulphatase) lies adjacent to an ATP-binding cassette transporter and a LysR type regulator, but well away from betBA, encoding enzymes for transformation of choline into glycine betaine. The consequences of such genetic layout of the functions for COS metabolism have...

Read the complete abstract on PubMed

Topics

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

Share to Betaine
Share to Choline
Share to Osmolar Concentration

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

Share to Osmotic Pressure

Share to Pseudomonas putida

Share to Sodium Chloride

Share to Sulfatases

Share to Sulfates

Source

Identifiers

PMID: 17116241
DOI: 10.1111/j.1365-2958.2006.05488.x

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

Uncoupling of choline-O-sulphate utilization from osmoprotection in Pseudomonas putida.PMID 17116241Read ↗

Presence of a gene encoding choline sulfatase in Sinorhizobium meliloti bet operon: choline-O-sulfate is metabolized into glycine betaine.Semantic proximity Read ↗

The diversity and functions of choline sulphatases in microorganisms.Semantic proximity Read ↗

The Sinorhizobium meliloti glycine betaine biosynthetic genes (betlCBA) are induced by choline and highly expressed in bacteroids.Semantic proximity Read ↗

Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD.Semantic proximity Read ↗

Characterization of the osmoprotectant transporter OpuC from Pseudomonas syringae and demonstration that cystathionine-beta-synthase domains are required for its osmoregulatory function.Semantic proximity Read ↗

Generation of a catR deficient mutant of P. putida KT2440 that produces cis, cis-muconate from benzoate at high rate and yield.Semantic proximity Read ↗

Halotolerant cyanobacterium Aphanothece halophytica contains a betaine transporter active at alkaline pH and high salinity.Semantic proximity Read ↗

The complex bet promoters of Escherichia coli: regulation by oxygen (ArcA), choline (BetI), and osmotic stress.Semantic proximity Read ↗

Isolation and characterization of ButA, a secondary glycine betaine transport system operating in Tetragenococcus halophila.Semantic proximity Read ↗

Resistance to serine in Bacillus subtilis: identification of the serine transporter YbeC and of a metabolic network that links serine and threonine metabolism.Semantic proximity Read ↗

Isolation, characterization, and expression of the Corynebacterium glutamicum betP gene, encoding the transport system for the compatible solute glycine betaine.Semantic proximity Read ↗

Regulatory properties and interaction of the C- and N-terminal domains of BetP, an osmoregulated betaine transporter from Corynebacterium glutamicum.Semantic proximity Read ↗

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