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

Activity-stability trade-off observed in variants at position 315 of the GH10 xylanase XynR.

Scientific reports - 2 Apr 2024

Nakamura Tomoka, Takita Teisuke, Kuwata Kohei, Mizutani Kimihiko, Mikami Bunzo, Nakamura Satoshi, Yasukawa Kiyoshi

Abstract excerpt

XynR is a thermostable alkaline GH10 xylanase, for which we have previously examined the effects of saturation mutagenesis at position 315 on enzyme alkaliphily, and found that at pH 10, the activities of variants could be ordered as follows: T315Q > T315S = T315N > T315H = wild-type XynR (WT) > 15 other variants. In this study, we sought to elucidate the mechanisms underlying the variable activity of these...

Read the complete abstract on PubMed

Topics

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

Share to Calcium Chloride
Share to Endo-1,4-beta Xylanases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Hydrogen-Ion Concentration

Share to Mutagenesis

Share to Mutation

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 38565938
DOI: 10.1038/s41598-024-57819-z
PMCID: PMC10987496

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

Activity-stability trade-off observed in variants at position 315 of the GH10 xylanase XynR.PMID 38565938Read ↗

Improvement of alkalophilicity of an alkaline xylanase Xyn11A-LC from Bacillus sp. SN5 by random mutation and Glu135 saturation mutagenesis.Semantic proximity Read ↗

Improving the Thermostability of Xylanase A from Bacillus subtilis by Combining Bioinformatics and Electrostatic Interactions Optimization.Semantic proximity Read ↗

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

High-temperature behavior of hyperthermostable Thermotoga maritima xylanase XYN10B after designed and evolved mutations.Semantic proximity Read ↗

Unleashing the Power of Evolution in Xylanase Engineering: Investigating the Role of Distal Mutation Regulation.Semantic proximity Read ↗

Thermostabilization of Bacillus subtilis GH11 xylanase by surface charge engineering.Semantic proximity Read ↗

Improvement of the catalytic performance of a hyperthermostable GH10 xylanase from Talaromyces leycettanus JCM12802.Semantic proximity Read ↗

Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface.Semantic proximity Read ↗

Improving the kinetic stability of a hyperthermostable β-mannanase by a rationally combined strategy.Semantic proximity Read ↗

Improvement of the optimum pH of Aspergillus niger xylanase towards an alkaline pH by site-directed mutagenesis.Semantic proximity Read ↗

Rational design of thermostability in bacterial 1,3-1,4-β-glucanases through spatial compartmentalization of mutational hotspots.Semantic proximity Read ↗

Enhancement in catalytic activity of Aspergillus niger XynB by selective site-directed mutagenesis of active site amino acids.Semantic proximity Read ↗

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