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

The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans.

The Journal of biological chemistry - 25 Mar 2016

Lafond Mickael, Sulzenbacher Gerlind, Freyd Thibaud, Henrissat Bernard, Berrin Jean-Guy, Garron Marie-Line

Abstract excerpt

In the Carbohydrate-Active Enzyme (CAZy) database, glycoside hydrolase family 5 (GH5) is a large family with more than 6,000 sequences. Among the 51 described GH5 subfamilies, subfamily GH5_26 contains members that display either endo-β(1,4)-glucanase or β(1,3;1,4)-glucanase activities. In this study, we focused on the GH5_26 enzyme fromSaccharophagus degradans(SdGluc5_26A), a marine bacterium known for its...

Read the complete abstract on PubMed

Topics

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

Share to Aquatic Organisms
Share to beta-Glucans

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

Share to Biocatalysis

Share to Gammaproteobacteria

Share to Glycoside Hydrolases

Share to Hydrolysis

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Source

Open in PubMed Open full text

Identifiers

PMID: 26755730
DOI: 10.1074/jbc.M115.695999
PMCID: PMC4807298

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

The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans.PMID 26755730Read ↗

Active site and laminarin binding in glycoside hydrolase family 55.Semantic proximity Read ↗

Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism.Semantic proximity Read ↗

Mutational and structural analyses of Caldanaerobius polysaccharolyticus Man5B reveal novel active site residues for family 5 glycoside hydrolases.Semantic proximity Read ↗

Spatially remote motifs cooperatively affect substrate preference of a ruminal GH26-type endo-β-1,4-mannanase.Semantic proximity Read ↗

Family 46 Carbohydrate-binding Modules Contribute to the Enzymatic Hydrolysis of Xyloglucan and β-1,3-1,4-Glucans through Distinct Mechanisms.Semantic proximity Read ↗

Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes.Semantic proximity Read ↗

Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.Semantic proximity Read ↗

Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module.Semantic proximity Read ↗

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

Structure-Function Analysis of a Mixed-linkage β-Glucanase/Xyloglucanase from the Key Ruminal Bacteroidetes Prevotella bryantii B(1)4.Semantic 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 ↗

Structural features of Aspergillus niger β-galactosidase define its activity against glycoside linkages.Semantic proximity Read ↗

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