Evidence map›Paper›PMID 30072664›Full record

ReviewBiology2018

Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.

Thomas Heine, Willem J H van Berkel, George Gassner, Karl-Heinz van Pée, Dirk Tischler

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Whole-genomic and transcriptomic analyses elucidateApplied and environmental microbiology · 2026
    Article
  3. Antifungal activity of the culture filtrate ofFrontiers in microbiology · 2026
    Article
  4. Article
  5. Gene cloning, phenol-responsive transcriptional profiling and recombinant protein characterization of phenol hydroxylase in Candida tropicalis GY8.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Activity-Based Protein Profiling of Bacterial Monooxygenases.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Identification of an indole biodegradation gene cluster fromFrontiers in bioengineering and biotechnology · 2022
    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

5 authors at 4 institutions in 3 countries.

Thomas HeineInstitute of Biosciences, Environmental Microbiology, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany. heinet@tu-freiberg.de.ORCID 0000-0002-7109-2788
Willem J H van BerkelLaboratory of Biochemistry, Wageningen University & Research, Stippeneng 4, 6708 WE Wageningen, The Netherlands. willem.vanberkel@wur.nl.ORCID 0000-0002-6551-2782
George GassnerDepartment of Chemistry and Biochemistry, San Francisco State University, 1600 Holloway Avenue, San Francisco, CA 94132, USA. gassner@sfsu.edu.
Karl-Heinz van PéeAllgemeine Biochemie, Technische Universität Dresden, 01062 Dresden, Germany. karl-heinz.van_pee@tu-dresden.de.
Dirk TischlerInstitute of Biosciences, Environmental Microbiology, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany. dirk.tischler@rub.de.ORCID 0000-0002-6288-2403
TU Bergakademie Freiberg · DESan Francisco State University · USTechnische Universität Dresden · DEWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single- or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent monooxygenases and describe their biotechnological relevance. Two-component FAD-dependent monooxygenases catalyze hydroxylation, epoxidation, and halogenation reactions and are physiologically involved in amino acid metabolism, mineralization of aromatic compounds, and biosynthesis of secondary metabolites. The monooxygenase component of these enzymes is strictly dependent on reduced FAD, which is supplied by the reductase component. More and more representatives of two-component FAD-dependent monooxygenases have been discovered and characterized in recent years, which has resulted in the identification of novel physiological roles, functional properties, and a variety of biocatalytic opportunities.

Indexed as

biocatalysisepoxidationflavin reductaseflavoprotein monooxygenaseshalogenationheteroatom oxidationhydroxylation

Identifiers

PMID30072664
PMCPMC6165268
OpenAlexW2885598475

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.