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

Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.

The Journal of biological chemistry - 2 May 2008

Gregg Katie J, Finn Ron, Abbott D Wade, Boraston Alisdair B

Abstract excerpt

The genomes of myonecrotic Clostridium perfringens isolates contain genes encoding a large and fascinating array of highly modular glycoside hydrolase enzymes. Although the catalytic activities of many of these enzymes are somewhat predictable based on their amino acid sequences, the functions of their abundant ancillary modules are not and remain poorly studied. Here, we present the structural and functional...

Read the complete abstract on PubMed

Topics

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

Share to Blood Group Antigens
Share to Calcium
Share to Carbohydrate Metabolism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Clostridium perfringens

Share to Crystallography, X-Ray

Share to Galactose

Share to Glycoside Hydrolases

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 18292090
DOI: 10.1074/jbc.M709865200
PMCID: PMC2335362

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

Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.PMID 18292090Read ↗

The Interaction of a Carbohydrate-binding Module from a Clostridium perfringens N-Acetyl-β-hexosaminidase with Its Carbohydrate ReceptorSemantic proximity Read ↗

The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site.Semantic proximity Read ↗

Carbohydrate Recognition by an Architecturally Complex α-N-Acetylglucosaminidase from Clostridium perfringensSemantic proximity Read ↗

Portrait of an Enzyme, a Complete Structural Analysis of a Multimodular β-N-Acetylglucosaminidase from Clostridium perfringensSemantic proximity Read ↗

The role of fucose-containing glycan motifs across taxonomic kingdomsSemantic proximity Read ↗

A Novel Carbohydrate-binding Module from Sugar Cane Soil Metagenome Featuring Unique Structural and Carbohydrate Affinity Properties.Semantic proximity Read ↗

Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.Semantic proximity Read ↗

Family 42 carbohydrate-binding modules display multiple arabinoxylan-binding interfaces presenting different ligand affinities.Semantic proximity Read ↗

The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes.Semantic proximity Read ↗

Investigating Host Microbiota Relationships Through Functional MetagenomicsSemantic proximity Read ↗

Bacteroides thetaiotaomicron generates diverse α-mannosidase activities through subtle evolution of a distal substrate-binding motif.Semantic proximity Read ↗

The Comparative Analysis of Genomic Diversity and Genes Involved in Carbohydrate Metabolism of Eighty-Eight Bifidobacterium pseudocatenulatum Isolates from Different Niches of ChinaSemantic proximity Read ↗

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