Evidence map›Paper›PMID 29776364›Full record

ArticleMicrobial cell factories2018

Identification, function, and application of 3-ketosteroid Δ1-dehydrogenase isozymes in Mycobacterium neoaurum DSM 1381 for the production of steroidic synthons.

Ruijie Zhang, Xiangcen Liu, Yushi Wang, Yuchang Han, Junsong Sun, Jiping Shi, Baoguo Zhang

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  6. Whole-Genome Analysis ofInternational journal of molecular sciences · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. 1,2-Hydrogenation and Transhydrogenation Catalyzed by 3-Ketosteroid ΔInternational journal of molecular sciences · 2022
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Universal capability of 3-ketosteroid ΔMicrobial cell factories · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. 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 2 institutions in 1 country.

Ruijie ZhangLab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, 201210, Shanghai, China.
Xiangcen LiuLab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, 201210, Shanghai, China.
Yushi WangLab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, 201210, Shanghai, China.
Yuchang HanLab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, 201210, Shanghai, China.
Junsong SunLab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, 201210, Shanghai, China.
Jiping ShiLab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, 201210, Shanghai, China. shijp@sari.ac.cn.
Baoguo ZhangLab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, 201210, Shanghai, China. zhangbg@sari.ac.cn.ORCID http://orcid.org/0000-0002-0800-0342
Chinese Academy of Sciences · CNShanghaiTech University · CN

Funding

the National Natural Science Foundation of China 41106125
6 · The paper itself

Abstract

background3-Ketosteroid-Δ1-dehydrogenase (KstD) is a key enzyme in the metabolic pathway for chemical modifications of steroid hormones. Only a few KstDs have thus far been characterized biochemically and applied for the production of steroidal pharmaceutical intermediates. Three KstDs, KstD1, KstD2, and KstD3, were identified in Mycobacterium neoaurum DSM 1381, and they shared up to 99, 85 and 97% amino acid identity with previously reported KstDs, respectively. In this paper, KstDs from M. neoaurum DSM 1381 were investigated and exemplified their potential application for industrial steroid transformation.

resultsThe recombinant KstD2 from Bacillus subtilis exhibited higher enzymatic activity when 4-androstene-3,17-dione (AD) and 22-hydroxy-23, 24-bisnorchol-4-ene-3-one (4HP) were used as the substrates, and resulted in specific activities of 22.40 and 19.19 U mg

conclusionsIn vitro assay employing the recombinant enzymes revealed that KstD2 was the most promising candidate for biocatalysis in biotransformation of AD. However, in vivo analysis showed that the cellular regulation of kstD1 was much more active than those of the other kstDs in response to the presence of phytosterols. Based on the findings above, we successfully constructed E. coli transformant BL21-kstD2 for ADD production from AD and M. neoaurum DSM 1381 ΔkstD1 strain for 4HP production using phytosterols as the substrate.

Indexed as

Bacterial ProteinsIsoenzymesMycobacteriumOxidoreductasesSteroids3-oxosteroid delta(1) dehydrogenaseBacterial ProteinsIsoenzymesOxidoreductasesSteroids1,4-Androstadiene-3,17-dione (ADD) steroids22-Hydroxy-23,24-bisnorchol-4-ene-3-one (4HP)3-Ketosteroid-∆1-dehydrogenaseMycobacterium

Identifiers

PMID29776364
PMCPMC5960168
OpenAlexW2803809638

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.