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

Mechanistic studies on PseB of pseudaminic acid biosynthesis: a UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase.

Bioorganic chemistry - 1 Dec 2008

Morrison James P, Schoenhofen Ian C, Tanner Martin E

Abstract excerpt

UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase (PseB) is a unique sugar nucleotide dehydratase that inverts the C-5'' stereocentre during conversion of UDP-N-acetylglucosamine to UDP-2-acetamido-2,6-dideoxy-beta-l-arabino-hexos-4-ulose. PseB catalyzes the first step in the biosynthesis of pseudaminic acid, which is found as a post-translational modification on the flagellin of Campylobacter jejuni and...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Campylobacter jejuni
Share to Helicobacter pylori

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydro-Lyases

Share to Ketones

Share to Oxygen

Share to Solvents

Source

Identifiers

PMID: 18845311
DOI: 10.1016/j.bioorg.2008.08.004

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

Mechanistic studies on PseB of pseudaminic acid biosynthesis: a UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase.PMID 18845311Read ↗

Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori.Semantic proximity Read ↗

Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways.Semantic proximity Read ↗

Structural Studies of FlaA1 from Helicobacter pylori Reveal the Mechanism for Inverting 4,6-Dehydratase ActivitySemantic proximity Read ↗

Mechanistic characterization of UDP-glucuronic acid 4-epimerase.Semantic proximity Read ↗

Mechanism and active site residues of GDP-fucose synthase.Semantic proximity Read ↗

Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni 81-176 using a focused metabolomics approach.Semantic proximity Read ↗

Structural and functional characterization of the Clostridium perfringens N-acetylmannosamine-6-phosphate 2-epimerase essential for the sialic acid salvage pathway.Semantic proximity Read ↗

Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori.Semantic proximity Read ↗

Significant catalytic roles for Glu47 and Gln 110 in all four of the C-C bond-making and -breaking steps of the reactions of acetohydroxyacid synthase II.Semantic proximity Read ↗

Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene.Semantic proximity Read ↗

A Unified Mechanism Reveals the Evolutionary Origin of Enoyl IsomerasesSemantic proximity Read ↗

Discovery of Cyanobacterial Natural Products Containing Fatty Acid ResiduesSemantic proximity Read ↗

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