Evidence map›Paper›PMID 36534341›Full record

ArticleThe protein journal2023

Enzymatic Characterization and Coenzyme Specificity Conversion of a Novel Dimeric Malate Dehydrogenase from Bacillus subtilis.

Ya-Dong Ge, Yi-Tian Guo, Lu-Lu Jiang, Hui-Hui Wang, Shao-Lin Hou, Feng-Zhi Su

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The protein journal, 2023. 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 42% 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, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. 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.

Ya-Dong GeCollege of Life Sciences, Anhui Normal University, Wuhu, 241000, People's Republic of China. geyd@ahnu.edu.cn.ORCID 0000-0002-2396-3139
Yi-Tian GuoCollege of Life Sciences, Anhui Normal University, Wuhu, 241000, People's Republic of China.
Lu-Lu JiangCollege of Life Sciences, Anhui Normal University, Wuhu, 241000, People's Republic of China.
Hui-Hui WangCollege of Life Sciences, Anhui Normal University, Wuhu, 241000, People's Republic of China.
Shao-Lin HouCollege of Life Sciences, Anhui Normal University, Wuhu, 241000, People's Republic of China.
Feng-Zhi SuCollege of Life Sciences, Anhui Normal University, Wuhu, 241000, People's Republic of China.
Anhui Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Malate is an important material to various industrials and clinical applications. Bacillus subtilis is a widely used biocatalyst tool for chemical production. However, the specific enzymatic properties of malate dehydrogenase from Bacillus subtilis (BsMDH) remain largely unknown. In the present study, BsMDH was cloned, recombinantly expressed and purified to test its enzymatic properties. The molecular weight of single unit of BsMDH was 34,869.7 Da. Matrix-Assisted Laser-Desorption Ionization-Time-of-Flight Mass Spectrometry and gel filtration analysis indicated that the recombinant BsMDH could form dimers. The k

Indexed as

CoenzymesNADBacillus subtilisKineticsMalate DehydrogenaseMalatesNADPCoenzymesMalate DehydrogenaseMalatesmalic acidNADNADPBacillus subtilisCoenzyme specificity conversionEnzymologyMalate dehydrogenaseMolecular evolution

Identifiers

PMID36534341
PMCPMC9761052
OpenAlexW4312056230

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.