Evidence map›Paper›PMID 30032434›Full record

ReviewApplied microbiology and biotechnology2018

Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.

Maciej Szaleniec, Agnieszka M Wojtkiewicz, Rita Bernhardt, Tomasz Borowski, Marina Donova

Erratum issuedOpen access · hybridAbstract readReview
In one paragraph

Review in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 8% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 108 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. The bile acid-gut microbiota-vitamin D axis: new insights into biliary atresia.Frontiers in cellular and infection microbiology · 2026
    Review
  6. Article
  7. Mycobacteriumabscessus CYP123 is a steroid hydroxylase with an implication in host infection.Drug metabolism and disposition: the biological fate of chemicals · 2025
    Article
  8. Cutaneous and Gut Dysbiosis in Alopecia Areata: A Review.JID innovations : skin science from molecules to population health · 2025
    Review
  9. Review
  10. Review
  11. Article
  12. Evolutionary formation of melatonin and vitamin D in early life forms: insects take centre stage.Biological reviews of the Cambridge Philosophical Society · 2024
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Bioconversion of vitamin DAMB Express · 2023
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Maciej SzaleniecJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239, Kraków, Poland. ncszalen@cyfronet.pl.ORCID http://orcid.org/0000-0002-7650-9263
Agnieszka M WojtkiewiczJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239, Kraków, Poland.
Rita BernhardtLehrstuhl für Biochemie, Universität des Saarlandes, Campus B2 2, 66123, Saarbrücken, Germany.
Tomasz BorowskiJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239, Kraków, Poland.
Marina DonovaG.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Oblast, 142290, Russia.
Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences · PLG. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms · RUSaarland University · DE

Funding

Polish National Center of Science SONATA UMO-2012/05/D/ST4/00277Russian Science Foundation N18-14-00361
6 · The paper itself

Abstract

The steroid superfamily includes a wide range of compounds that are essential for living organisms of the animal and plant kingdoms. Structural modifications of steroids highly affect their biological activity. In this review, we focus on hydroxylation of steroids by bacterial hydroxylases, which take part in steroid catabolic pathways and play an important role in steroid degradation. We compare three distinct classes of metalloenzymes responsible for aerobic or anaerobic hydroxylation of steroids, namely: cytochrome P450, Rieske-type monooxygenase 3-ketosteroid 9α-hydroxylase, and molybdenum-containing steroid C25 dehydrogenases. We analyze the available literature data on reactivity, regioselectivity, and potential application of these enzymes in organic synthesis of hydroxysteroids. Moreover, we describe mechanistic hypotheses proposed for all three classes of enzymes along with experimental and theoretical evidences, which have provided grounds for their formulation. In case of the 3-ketosteroid 9α-hydroxylase, such a mechanistic hypothesis is formulated for the first time in the literature based on studies conducted for other Rieske monooxygenases. Finally, we provide comparative analysis of similarities and differences in the reaction mechanisms utilized by bacterial steroid hydroxylases.

Indexed as

AnimalsBacterial ProteinsCatalysisHumansHydroxylationSteroid HydroxylasesSteroidsBacterial ProteinsSteroid HydroxylasesSteroids3-ketosteroid 9α-hydroxylaseCytochrome P450Steroid C25 dehydrogenaseSteroid hydroxylation

Identifiers

PMID30032434
PMCPMC6153880
OpenAlexW2884477296

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.