Evidence map›Paper›PMID 29779661›Full record

ArticleMethods in enzymology2018

Characterization and Biochemical Assays of Streptomyces Vanadium-Dependent Chloroperoxidases.

Shaun M K McKinnie, Zachary D Miles, Bradley S Moore

Abstract read
In one paragraph

Article in Methods in enzymology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Thermotolerant class A acid phosphatase active across broad pH range and diverse substrates.Protein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. MAR4Journal of natural products · 2024
    Review
  10. Article
  11. Enzymatic Halogenation of Terminal Alkynes.Journal of the American Chemical Society · 2023
    Article
  12. Article
  13. 30th Annual GPPharmaceuticals (Basel, Switzerland) · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

3 authors.

Shaun M K McKinnieCenter for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California at San Diego, La Jolla, CA, United States.
Zachary D MilesCenter for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California at San Diego, La Jolla, CA, United States.
Bradley S MooreCenter for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California at San Diego, La Jolla, CA, United States; Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, CA, United States. Electronic address: bsmoore@ucsd.edu.

Funding

ENGINEERING DIVERSITY WITH ENTEROCIN BIOSYNTHESIS GENER01AI047818 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI MOORE, BRADLEY S · 2000 to 2022
$5.2M
NIAID NIH HHS R01 AI047818
6 · The paper itself

Abstract

Vanadium-dependent haloperoxidases (VHPOs) are fascinating enzymes that facilitate electrophilic halogen incorporation into electron-rich substrates, simply requiring vanadate, a halide source, and cosubstrate hydrogen peroxide for activity. Initially characterized in fungi and red algae, VHPOs were long believed to have limited regio-, chemo-, and enantioselectivity in the production of halogenated metabolites. However, the recent discovery of homologues in the biosynthetic gene clusters of the stereoselectively halogenated meroterpenoids from marine-derived Streptomyces bacteria has revised this paradigm. Their intriguing transformations have both enhanced and contributed to the fields of synthetic organic and natural product chemistry. We, herein, describe the expression, purification, and chemical assays of two characterized vanadium-dependent chloroperoxidase enzymes (NapH1 and Mcl24), and one homologue devoid of chlorination activity (NapH3), involved in the biosyntheses of halogenated meroterpenoid products.

Indexed as

Bacterial ProteinsBiochemistryChloride PeroxidaseCyclizationCyclohexanonesMolecular BiologyNaphthoquinonesRecombinant ProteinsSesterterpenesStreptomycesVanadiumBacterial ProteinsChloride PeroxidasechlorodimedoneCyclohexanonesmerochlorin Amerochlorin BnaphthomevalinNaphthoquinonesnapyradiomycin A1Recombinant ProteinsSesterterpenesVanadiumvanadium chloroperoxidaseActinomycesBiosynthesisChlorinationHalogenaseMeroterpenoidNatural productsRearrangementStereoselectiveStreptomycesVanadium

Identifiers

PMID29779661
PMCPMC6205230

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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.