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

Change of the donor substrate specificity of Clostridium difficile toxin B by site-directed mutagenesis.

The Journal of biological chemistry - 11 Nov 2005

Jank Thomas, Reinert Dirk J, Giesemann Torsten, Schulz Georg E, Aktories Klaus

Abstract excerpt

The large cytotoxins of Clostridia species glycosylate and thereby inactivate small GTPases of the Rho family. Clostridium difficile toxins A and B and Clostridium sordellii lethal toxin use UDP-glucose as the donor for glucosylation of Rho/Ras GTPases. In contrast, alpha-toxin from Clostridium novyi N-acetylglucosaminylates Rho GTPases by using UDP-N-acetylglucosamine as a donor substrate. Based on the crystal...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Toxins
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Kinetics

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Share to Substrate Specificity

Source

Identifiers

PMID: 16157585
DOI: 10.1074/jbc.M506836200

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

Change of the donor substrate specificity of Clostridium difficile toxin B by site-directed mutagenesis.PMID 16157585Read ↗

Involvement of a conserved tryptophan residue in the UDP-glucose binding of large clostridial cytotoxin glycosyltransferases.Semantic proximity Read ↗

Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects.Semantic proximity Read ↗

UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii.Semantic proximity Read ↗

Identification of an Essential Region for Translocation of Clostridium difficile Toxin B.Semantic proximity Read ↗

Structural basis for the function of Clostridium difficile toxin B.Semantic proximity Read ↗

Processing of Clostridium difficile toxinsSemantic proximity Read ↗

The glucosyltransferase activity of C. difficile Toxin B is required for disease pathogenesisSemantic proximity Read ↗

Defective mutations within the translocation domain of Clostridium difficile toxin B impair disease pathogenesis.Semantic proximity Read ↗

A glutamic acid 3-methyltransferase encoded by an accessory gene locus important for daptomycin biosynthesis in Streptomyces roseosporus.Semantic proximity Read ↗

Mutational analysis of the enzymatic domain of Clostridium difficile toxin B reveals novel inhibitors of the wild-type toxin.Semantic proximity Read ↗

The identity determinants required for the discrimination between tRNAGlu and tRNAAsp by glutamyl-tRNA synthetase from Escherichia coli.Semantic proximity Read ↗

Conserved Arginines at the P-Protein Stalk Binding Site and the Active Site Are Critical for Ribosome Interactions of Shiga Toxins but Do Not Contribute to Differences in the Affinity of the A1 Subunits for the Ribosome.Semantic proximity Read ↗

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