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

Variants of the beta 1,3-galactosyltransferase CgtB from the bacterium Campylobacter jejuni have distinct acceptor specificities.

Glycobiology - 1 Dec 2007

Bernatchez Stéphane, Gilbert Michel, Blanchard Marie-Claude, Karwaski Marie-France, Li Jianjun, Defrees Shawn, Wakarchuk Warren W

Abstract excerpt

The gene clusters encoding the lipooligosaccharide biosynthesis glycosyltransferases from Campylobacter jejuni have previously been divided in eight classes based on their genetic organization. Here, three variants of the beta1,3-galactosyltransferase CgtB from two classes were purified as fusions with the maltose-binding protein (MalE) from Escherichia coli and their acceptor preference was determined. The...

Read the complete abstract on PubMed

Topics

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

Share to Campylobacter jejuni
Share to Galactosyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Enzymologic

Share to Glycosylation

Share to Glycosyltransferases

Share to Mass Spectrometry

Share to Polysaccharides

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Identifiers

PMID: 17766267
DOI: 10.1093/glycob/cwm090

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Variants of the beta 1,3-galactosyltransferase CgtB from the bacterium Campylobacter jejuni have distinct acceptor specificities.PMID 17766267Read ↗

Origin, evolution, and distribution of the molecular machinery for biosynthesis of sialylated lipooligosaccharide structures in <i>Campylobacter coli</i>Semantic proximity Read ↗

Characterization of the structurally diverse N-linked glycans of Campylobacter species.Semantic proximity Read ↗

Genetics behind the biosynthesis of nonulosonic acid containing lipooligosaccharides in <i>Campylobacter coli</i>Semantic proximity Read ↗

Increased efficiency of Campylobacter jejuni N-oligosaccharyltransferase PglB by structure-guided engineering.Semantic proximity Read ↗

Identifying the targets and functions of N -linked protein glycosylation in Campylobacter jejuniSemantic proximity Read ↗

Comparative genomics analysis of completely sequenced microbial genomes reveals the ubiquity of N-linked glycosylation in prokaryotes.Semantic proximity Read ↗

Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: tool to study protein N-glycosylation pathways.Semantic proximity Read ↗

The Corynebacterium glutamicum gene pmt encoding a glycosyltransferase related to eukaryotic protein-O-mannosyltransferases is essential for glycosylation of the resuscitation promoting factor (Rpf2) and other secreted proteins.Semantic proximity Read ↗

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.Semantic proximity Read ↗

Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway.Semantic proximity Read ↗

Identification of an alpha(1-->6) mannopyranosyltransferase (MptA), involved in Corynebacterium glutamicum lipomanann biosynthesis, and identification of its orthologue in Mycobacterium tuberculosis.Semantic proximity Read ↗

Engineering β-1,4-galactosyltransferase to Enhance Lacto-N-neotetraose Production in Corynebacterium glutamicumSemantic proximity Read ↗

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