Evidence map›Paper›PMID 33465708›Full record

ArticleThe Journal of biological chemistry

Dissecting the low catalytic capability of flavin-dependent halogenases.

Aisaraphon Phintha, Kridsadakorn Prakinee, Aritsara Jaruwat, Narin Lawan, Surawit Visitsatthawong, Chadaporn Kantiwiriyawanitch, Warangkhana Songsungthong, Duangthip Trisrivirat, Pirom Chenprakhon, Adrian Mulholland and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.1field-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

25 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  3. Peptidic Tryptophan Halogenation by a Promiscuous Flavin-Dependent Enzyme.Angewandte Chemie (International ed. in English) · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Balance between photoreduction efficiency, cofactor affinity, and allosteric coupling of halogenase flavoenzymes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    Article
  10. Article
  11. Peptide halogenation biochemistry: interfacing pharmaceutical deliverables with chemical innovation.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Enzymatic Halogenation of Terminal Alkynes.Journal of the American Chemical Society · 2023
    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

13 authors at 6 institutions in 3 countries.

Aisaraphon PhinthaDepartment of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok, Thailand; School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.
Kridsadakorn PrakineeSchool of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.
Aritsara JaruwatBiomolecular Analysis and Application Research Team, National Center for Genetic Engineering and Biotechnology, Klong Luang, Pathumthani, Thailand.
Narin LawanDepartment of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.
Surawit VisitsatthawongSchool of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.
Chadaporn KantiwiriyawanitchSchool of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.
Warangkhana SongsungthongBiomolecular Analysis and Application Research Team, National Center for Genetic Engineering and Biotechnology, Klong Luang, Pathumthani, Thailand.
Duangthip TrisriviratSchool of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.
Pirom ChenprakhonInstitute for Innovative Learning, Mahidol University, Nakhon Pathom, Thailand.
Adrian MulhollandCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol, UK.
Karl-Heinz van PéeGeneral Biochemistry, Faculty of Chemistry and Food Chemistry, Technical University of Dresden, Dresden, Germany.
Penchit ChitnumsubBiomolecular Analysis and Application Research Team, National Center for Genetic Engineering and Biotechnology, Klong Luang, Pathumthani, Thailand. Electronic address: penchit@biotec.or.th.
Pimchai ChaiyenDepartment of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok, Thailand; School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand. Electronic address: pimchai.chaiyen@vistec.ac.th.
Vidyasirimedhi Institute of Science and Technology · THMahidol University · THNational Center for Genetic Engineering and Biotechnology · THChiang Mai University · THTechnische Universität Dresden · DEUniversity of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

Although flavin-dependent halogenases (FDHs) are attractive biocatalysts, their practical applications are limited because of their low catalytic efficiency. Here, we investigated the reaction mechanisms and structures of tryptophan 6-halogenase (Thal) from Streptomyces albogriseolus using stopped-flow, rapid-quench flow, quantum/mechanics molecular mechanics calculations, crystallography, and detection of intermediate (hypohalous acid [HOX]) liberation. We found that the key flavin intermediate, C4a-hydroperoxyflavin (C4aOOH-FAD), formed by Thal and other FDHs (tryptophan 7-halogenase [PrnA] and tryptophan 5-halogenase [PyrH]), can react with I

Indexed as

CatalysisCrystallography, X-RayFlavin-Adenine DinucleotideFlavinsHalogenationHydrogen PeroxideKineticsModels, MolecularOxidoreductasesProtein ConformationFlavin-Adenine DinucleotideFlavinsHydrogen PeroxideOxidoreductasestryptophan halogenaseflavin monooxygenasehalogenasekineticsQM/MM calculationsstopped-flowX-ray structures

Identifiers

PMID33465708
PMCPMC7948982
OpenAlexW3099097710

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.