Evidence map›Paper›PMID 35922648›Full record

ArticleBiotechnology letters2022

Improvement of the catalytic performance of glycerol kinase from Bacillus subtilis by chromosomal site-directed mutagenesis.

Guanglu Wang, Mengyuan Wang, Lanxi Liu, Xiaohan Hui, Bingyang Wang, Ke Ma, Xuepeng Yang

Abstract read
PubMed Publisher
In one paragraph

Article in Biotechnology letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Metabolic Engineering Strategy forFoods (Basel, Switzerland) · 2025
    Review
  3. Enhanced nattokinase production byFrontiers in microbiology · 2025
    Article
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

7 authors at 1 institution in 1 country.

Guanglu Wang *Laboratory of Biotransformation and Biocatalysis, School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou, Dongfeng Road 5, Henan, 450000, People's Republic of China.
Mengyuan Wang *Laboratory of Biotransformation and Biocatalysis, School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou, Dongfeng Road 5, Henan, 450000, People's Republic of China.
Lanxi LiuLaboratory of Biotransformation and Biocatalysis, School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou, Dongfeng Road 5, Henan, 450000, People's Republic of China.
Xiaohan HuiLaboratory of Biotransformation and Biocatalysis, School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou, Dongfeng Road 5, Henan, 450000, People's Republic of China.
Bingyang WangLaboratory of Biotransformation and Biocatalysis, School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou, Dongfeng Road 5, Henan, 450000, People's Republic of China.
Ke MaLaboratory of Biotransformation and Biocatalysis, School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou, Dongfeng Road 5, Henan, 450000, People's Republic of China.
Xuepeng YangLaboratory of Biotransformation and Biocatalysis, School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou, Dongfeng Road 5, Henan, 450000, People's Republic of China. yangxuepeng@zzuli.edu.cn.ORCID http://orcid.org/0000-0003-2923-7629
Zhengzhou University of Light Industry · CN

Funding

Joint Funds of the National Natural Science Foundation of China U1904101Key Research Projects of the Science and Technology Department of Henan Province 182102310607Key Research Projects of the Science and Technology Department of Henan Province 202102310021
6 · The paper itself

Abstract

Glycerol kinase is the key enzyme in glycerol metabolism, and its catalytic efficiency has an important effect on glycerol utilization. Based on an analysis of the glycerol utilization pathway and regulation mechanism in B. subtilis, we conducted site-directed mutagenesis of the key glycerol kinase gene (glpK) on the chromosome to improve the glycerol utilization efficiency of Bacillus subtilis. Recombinant wild-type Bacillus subtilis glycerol kinase (BsuGlpK

Indexed as

Bacillus subtilisGlycerol KinaseChromosomesEscherichia coliGlycerolMutagenesis, Site-DirectedGlycerolGlycerol KinaseBacillus subtilisGlycerol kinaseSite-directed mutagenesis

Identifiers

PMID35922648
OpenAlexW4289653832

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.