Evidence map›Paper›PMID 37537629›Full record

ArticleBiotechnology for biofuels and bioproducts2023

Alanine dehydrogenases from four different microorganisms: characterization and their application in L-alanine production.

Pengfei Gu, Qianqian Ma, Shuo Zhao, Qiang Li, Juan Gao

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels and bioproducts, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Efficient biosynthesis of D/L-alanine in the recombinantFrontiers in bioengineering and biotechnology · 2024
    Article
  4. Optimizing Hexose Utilization Pathways ofInternational journal of molecular sciences · 2023
    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

5 authors at 1 institution in 1 country.

Pengfei Gu *School of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China. bio_gupf@ujn.edu.cn.
Qianqian Ma *School of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China.
Shuo Zhao *School of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China.
Qiang LiSchool of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China.
Juan GaoSchool of Biological Science and Technology, University of Jinan, Jinan, 250022, People's Republic of China. bio_gaoj@ujn.edu.cn.
University of Jinan · CN

Funding

Key R&D Program of Shandong Province, China 2022SFGC0102National Natural Science Foundation of China 32070111National Natural Science Foundation of China 32270093Rizhao Science and Technology Innovation Project 2020CXZX1206the Higher Educational Science and Technology Program of Jinan City 2021GXRC088the Innovation Capability Improvement Project of technology-based medium and small enterprises in Shandong Province 2021TSGC1247the Science and Technology Program of the University of Jinan XKY2028
6 · The paper itself

Abstract

backgroundAlanine dehydrogenase (AlaDH) belongs to oxidoreductases, and it exists in several different bacteria species and plays a key role in microbial carbon and nitrogen metabolism, spore formation and photosynthesis. In addition, AlaDH can also be applied in biosynthesis of L-alanine from cheap carbon source, such as glucose.

resultsTo achieve a better performance of L-alanine accumulation, system evaluation and comparison of different AlaDH with potential application value are essential. In this study, enzymatic properties of AlaDH from Bacillus subtilis 168 (BsAlaDH), Bacillus cereus (BcAlaDH), Mycobacterium smegmatis MC

conclusionsEnzyme assay, biochemical characterization and structure analysis of BsAlaDH, BcAlaDH, MsAlaDH and GsAlaDH were carried out. In addition, application potential of these four AlaDHs in L-alanine productions were explored. The strategies here can be applied for developing L-alanine producing strains with high titers.

Indexed as

Alanine dehydrogenaseEscherichia coliL-alanineMetabolic engineering

Identifiers

PMID37537629
PMCPMC10401832
OpenAlexW4385563382

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.