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

Identification of the cellulose-binding domain of a Bacillus subtilis endoglucanase distinct from its catalytic domain.

Bioscience, biotechnology, and biochemistry - 1 Feb 1993

Park J S, Nakamura A, Horinouchi S, Beppu T

Abstract excerpt

The endoglucanase (BSC) from Bacillus subtilis IFO 3034, which shows no ability to hydrolyze microcrystalline cellulose, was found to bind to Avicel. Ninety-eight amino acids-truncation at the COOH-terminus of BSC did not abolish the carboxymethyl cellulose (CMC)-hydrolyzing ability, but removed the Avicel-binding ability. These data suggested the presence of an Avicel-binding domain at the COOH-terminus of BSC,...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Base Sequence
Share to Catalysis

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

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Plasmids

Share to Protein Binding

Source

Identifiers

PMID: 7763494
DOI: 10.1271/bbb.57.260

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

Identification of the cellulose-binding domain of a Bacillus subtilis endoglucanase distinct from its catalytic domain.PMID 7763494Read ↗

Enhancing the catalytic activity of a GH5 processive endoglucanase from Bacillus subtilis BS-5 by site-directed mutagenesis.Semantic proximity Read ↗

Molecular and biochemical analyses of CbCel9A/Cel48A, a highly secreted multi-modular cellulase by Caldicellulosiruptor bescii during growth on crystalline cellulose.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 ↗

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

Extra tyrosine in the carbohydrate-binding module of Irpex lacteus Xyn10B enhances its cellulose-binding ability.Semantic proximity Read ↗

Structure features of GH10 xylanase from Caldicellulosiruptor bescii: implication for its thermophilic adaption and substrate binding preference.Semantic proximity Read ↗

Functional and structural investigation of a novel β-mannanase BaMan113A from Bacillus sp. N16-5.Semantic proximity Read ↗

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

The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis.Semantic proximity Read ↗

Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose.Semantic proximity Read ↗

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

Analysis of the putative substrate binding region of hyperthermophilic endoglucanase from Pyrococcus horikoshii.Semantic proximity Read ↗

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