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

Structural and catalytic roles of amino acid residues located at substrate-binding pocket in Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase.

Proteins - 1 Oct 2010

Chen Je-Hsin, Tsai Li-Chu, Huang Hsiao-Chuan, Shyur Lie-Fen

Abstract excerpt

We created 12 mutant enzymes (E11L, F40I, Y42L, N44L, N44Q, E47I, L62G, K64A, K64M, R137M, R137Q, and N139A) from the truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase (TF-glucanase). The enzymes were used to investigate the structural and catalytic roles of specific amino acid residues located at the catalytic pocket and having direct interactions with glucose subsites of the product...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Biocatalysis
Share to Cellulose

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Glycoside Hydrolases

Share to Protein Structure, Secondary

Share to Spectrometry, Fluorescence

Share to Substrate Specificity

Source

Identifiers

PMID: 20635417
DOI: 10.1002/prot.22798

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

Structural and catalytic roles of amino acid residues located at substrate-binding pocket in Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase.PMID 20635417Read ↗

Directed mutagenesis of apecific active site residues on Fibrobacter succinogenes 1,3-1,4-beta -D-glucanase significantly affects catalysis and enzyme structural stability.Semantic proximity Read ↗

Rational design to improve thermostability and specific activity of the truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase.Semantic proximity Read ↗

A multifunctional α-amylase BSGH13 from Bacillus subtilis BS-5 possessing endoglucanase and xylanase activities.Semantic proximity Read ↗

Insights into the Catalytic Mechanism of a Novel XynA and Structure-Based Engineering for Improving Bifunctional Activities.Semantic proximity Read ↗

Identification and Mutation Analysis of Nonconserved Residues on the TIM-Barrel Surface of GH5_5 Cellulases for Catalytic Efficiency and Stability Improvement.Semantic proximity Read ↗

Improving enzyme activity of glucosamine-6-phosphate synthase by semi-rational design strategy and computer analysis.Semantic proximity Read ↗

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

Mechanistic insights into activity-enhancing mutations from comparative analysis of two Bacillus subtilis GH11 xylanases.Semantic proximity Read ↗

Functional dissection of the N-terminal sequence of Clostridium sp. G0005 glucoamylase: identification of components critical for folding the catalytic domain and for constructing the active site structure.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 ↗

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

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

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