Evidence map›Paper›PMID 32601959›Full record

ArticleBiotechnology letters2020

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

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

Abstract read
PubMed Publisher
In one paragraph

Article in Biotechnology letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 46% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Synthetic Biology Approaches to Enzymology in Food and Agriculture Systems.Journal of agricultural and food chemistry · 2026
    Review
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Piwu Li *State Key Laboratory of Biobased Material and Green Papermaking (LBMP) (Qilu University of Technology), Jinan, 250353, Shandong, People's Republic of China.
Kang Li *Key Laboratory of Shandong Microbial Engineering, QILU University of Technology (Shandong Academy of Sciences), Jinan, 250353, Shandong, People's Republic of China.
Xu LiKey Laboratory of Shandong Microbial Engineering, QILU University of Technology (Shandong Academy of Sciences), Jinan, 250353, Shandong, People's Republic of China.
Fei ZhaoKey Laboratory of Shandong Microbial Engineering, QILU University of Technology (Shandong Academy of Sciences), Jinan, 250353, Shandong, People's Republic of China.
Ruiming WangState Key Laboratory of Biobased Material and Green Papermaking (LBMP) (Qilu University of Technology), Jinan, 250353, Shandong, People's Republic of China.
Junqing WangState Key Laboratory of Biobased Material and Green Papermaking (LBMP) (Qilu University of Technology), Jinan, 250353, Shandong, People's Republic of China. wjqtt.6082@163.com.ORCID http://orcid.org/0000-0001-9862-2366
Qilu University of Technology · CN

Funding

Cultivation Project of Shandong Synthetic Biotechnology Innovation Center sdsynbio-2018-PY-02Focus on Research and Development Plan in Shandong Province 2018YFJH0401Innovative Research Group Project of the National Natural Science Foundation of China (CN) 31801527Major Program of National Natural Science Foundation of Shandong ZR2017ZB0208Major Science and Technology Projects in Shandong Province 2016CYJS07A01Shandong Provincial Natural Science Foundation ZR2016CB04Taishan industry leading talent tscy20180103
6 · The paper itself

Abstract

objectiveTo improve enzyme activity of Glucosamine-6-phosphate synthase (Glms) of Bacillus subtilis by site saturation mutagenesis at Leu

resultsThe results indicated that L

conclusionWe successfully improved BsGlms activity through computer simulation and site saturation mutagenesis. This combination of methodologies may fit into an efficient workflow for improving Glms and other proteins activity.

Indexed as

Bacillus subtilisBacterial ProteinsComputer SimulationGlucosamineGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)Models, MolecularMolecular Dynamics SimulationMutationStructural Homology, ProteinBacterial ProteinsGlucosamineGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)Computer simulationEnzyme activityGlucosamine-6-phosphate synthaseMolecular dynamics simulationSite saturation mutagenesis

Identifiers

PMID32601959
OpenAlexW3037343202

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.