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

Increased activity of β-glucuronidase variants produced by site-directed mutagenesis.

Enzyme and microbial technology - 1 Feb 2018

Zhang Xiaolei, Sitasuwan Pongkwan, Horvath Gary, Yang Jia, Nie Yuzhe, Marinova Margarita, Lee L Andrew, Wang Qian

Abstract excerpt

β-glucuronidase (BGus) is an essential glycosyl hydrolase which has been widely used in biological and biomedical applications. In this paper, we report the construction and screening of nineteen Escherichia coli BGus (EBGus) mutants using site-directed mutagenesis. The mutants G559N, G559S and G559T showed a 3-5 fold increase in enzyme activity in comparison to wild type EBGus. In particular, G559S, with the...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Glucuronidase

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Source

Identifiers

PMID: 29224622
DOI: 10.1016/j.enzmictec.2017.09.005

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

Increased activity of β-glucuronidase variants produced by site-directed mutagenesis.PMID 29224622Read ↗

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

Met349 Mutations Enhance the Activity of 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02.Semantic proximity Read ↗

Gly343 mutation enhances gentiobiose conversion efficiency of GH3 family β-glucosidase from Thermotoga maritima STB25.Semantic proximity Read ↗

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

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

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

Directed evolution of a glycosynthase from Agrobacterium sp. increases its catalytic activity dramatically and expands its substrate repertoire.Semantic proximity Read ↗

Structural features of Aspergillus niger β-galactosidase define its activity against glycoside linkages.Semantic proximity Read ↗

Specificity Enhancement of Glutenase Bga1903 Toward Celiac Disease-Eliciting Pro-immunogenic Peptides via Active-Site ModificationSemantic proximity Read ↗

Characterization of the inserted mutagenesis dextransucrases from Leuconostoc mesenteroides 0326 to produce hyperbranched dextran.Semantic proximity Read ↗

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

Mutagenesis for Improvement of Activity and Stability of Prolyl Aminopeptidase from Aspergillus oryzae.Semantic proximity Read ↗

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