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

Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase 1.

FEBS letters - 22 Dec 2007

Takashima Shou, Ohno Mitsuhiro, Hidaka Makoto, Nakamura Akira, Masaki Haruhiko, Uozumi Takeshi

Abstract excerpt

The cellulose-binding domains (CBDs) of fungal cellulases interact with crystalline cellulose through their hydrophobic flat surface formed by three conserved aromatic amino acid residues. To analyze the functional importance of these residues, we constructed CBD mutants of cellobiohydrolase 1 (CBH1) of the thermophilic fungus Humicola grisea, and examined their cellulose-binding ability and enzymatic activities....

Read the complete abstract on PubMed

Topics

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

Share to Cellulose
Share to Chromatography

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

Share to Hydrophobic and Hydrophilic Interactions

Share to Mitosporic Fungi

Share to Models, Molecular

Share to Mutant Proteins

Share to Protein Structure, Tertiary

Share to Sequence Alignment

Source

Identifiers

PMID: 18061578
DOI: 10.1016/j.febslet.2007.11.068

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

Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase 1.PMID 18061578Read ↗

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

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

Importance of exposed aromatic residues in chitinase B from Serratia marcescens 2170 for crystalline chitin hydrolysis.Semantic proximity Read ↗

Effects of noncatalytic residue mutations on substrate specificity and ligand binding of Thermobifida fusca endocellulase cel6A.Semantic proximity Read ↗

Mutation of active site residues in the chitin-binding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay.Semantic proximity Read ↗

Effects of pH and high ionic strength on the adsorption and activity of native and mutated cellobiohydrolase I from Trichoderma reesei.Semantic proximity Read ↗

Brittle Culm1, a COBRA-like protein, functions in cellulose assembly through binding cellulose microfibrils.Semantic proximity Read ↗

The carbohydrate-binding module (CBM)-like sequence is crucial for rice CWA1/BC1 function in proper assembly of secondary cell wall materials.Semantic proximity Read ↗

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

Identification of amino acids responsible for processivity in a Family 1 carbohydrate-binding module from a fungal cellulase.Semantic proximity Read ↗

Crystal structures of the catalytic domain of a novel glycohydrolase family 23 chitinase from Ralstonia sp. A-471 reveals a unique arrangement of the catalytic residues for inverting chitin hydrolysis.Semantic proximity Read ↗

Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study.Semantic proximity Read ↗

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