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

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

Biotechnology letters - 1 Nov 2020

Li Piwu, Li Kang, Li Xu, Zhao Fei, Wang Ruiming, Wang Junqing

Abstract excerpt

OBJECTIVE: To improve enzyme activity of Glucosamine-6-phosphate synthase (Glms) of Bacillus subtilis by site saturation mutagenesis at Leu593, Ala594, Lys595, Ser596 and Val597 based on computer-aided semi-rational design. RESULTS: The results indicated that L593S had the greatest effect on the activity of BsGlms and the enzyme activity increased from 5 to 48 U/mL. The mutation of L593S increased the yield of...

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 Bacterial Proteins

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

Share to Computer Simulation

Share to Glucosamine

Share to Models, Molecular

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Structural Homology, Protein

Source

Identifiers

PMID: 32601959
DOI: 10.1007/s10529-020-02949-3

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

Improving enzyme activity of glucosamine-6-phosphate synthase by semi-rational design strategy and computer analysis.PMID 32601959Read ↗

[Improving the thermal stability of Bacillus subtilis lipase based on multiple computational design strategies].Semantic proximity Read ↗

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

Computational design of new enzymes for hydrolysis and synthesis of third-generation cephalosporin antibiotics.Semantic proximity Read ↗

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

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

Enhancement of glutaminase production through protein design and host strain modification in Bacillus amyloliquefaciens.Semantic proximity Read ↗

B-factor-saturation mutagenesis as a strategy to increase the thermostability of α-L-rhamnosidase from Aspergillus terreus.Semantic proximity Read ↗

Enhanced Thermostability and Molecular Insights for l -Asparaginase from Bacillus licheniformis via Structure- and Computation-Based Rational DesignSemantic proximity Read ↗

Enhancing PgUGT activity and thermostability via mutation site screening aided by molecular docking structure and computer-aided design for efficient industrial synthesis of rebaudioside D.Semantic proximity Read ↗

Rational design of a thermophilic β-mannanase fromBacillus subtilis TJ-102 to improve its thermostability.Semantic proximity Read ↗

Integrated computer-aided drug design and biophysical simulation approaches to determine natural anti-bacterial compounds for Acinetobacter baumanniiSemantic proximity Read ↗

A study of targeted mutation of l-rhamnose isomerase to improve the conversion efficiency of D-allose.Semantic proximity Read ↗

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