Evidence map›Paper›PMID 34737365›Full record

ArticleScientific reports2021

Genetic fusion of P450 BM3 and formate dehydrogenase towards self-sufficient biocatalysts with enhanced activity.

Arsenij Kokorin, Pavel D Parshin, Patrick J Bakkes, Anastasia A Pometun, Vladimir I Tishkov, Vlada B Urlacher

Abstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. P450 Fusion Protein Expressed inMolecules (Basel, Switzerland) · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

6 authors.

Arsenij KokorinInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, 40225, Düsseldorf, Germany.
Pavel D ParshinDepartment of Chemistry, Lomonosov Moscow State University, 119991, Moscow, Russian Federation.
Patrick J BakkesInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, 40225, Düsseldorf, Germany.
Anastasia A PometunDepartment of Chemistry, Lomonosov Moscow State University, 119991, Moscow, Russian Federation.
Vladimir I TishkovDepartment of Chemistry, Lomonosov Moscow State University, 119991, Moscow, Russian Federation.
Vlada B UrlacherInstitute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, 40225, Düsseldorf, Germany. vlada.urlacher@uni-duesseldorf.de.

Funding

European Regional Development Fund 34.EFRE-0300095/1703FI04Russian Science Foundation 18-74-0014
6 · The paper itself

Abstract

Fusion of multiple enzymes to multifunctional constructs has been recognized as a viable strategy to improve enzymatic properties at various levels such as stability, activity and handling. In this study, the genes coding for cytochrome P450 BM3 from B. megaterium and formate dehydrogenase from Pseudomonas sp. were fused to enable both substrate oxidation catalyzed by P450 BM3 and continuous cofactor regeneration by formate dehydrogenase within one construct. The order of the genes in the fusion as well as the linkers that bridge the enzymes were varied. The resulting constructs were compared to individual enzymes regarding substrate conversion, stability and kinetic parameters to examine whether fusion led to any substantial improvements of enzymatic properties. Most noticeably, an activity increase of up to threefold was observed for the fusion constructs with various substrates which were partly attributed to the increased diflavin reductase activity of the P450 BM3. We suggest that P450 BM3 undergoes conformational changes upon fusion which resulted in altered properties, however, no NADPH channeling was detected for the fusion constructs.

Indexed as

Bacillus megateriumBacterial ProteinsCatalysisCytochrome P-450 Enzyme SystemEnzymesFormate DehydrogenasesNADPNADPH-Ferrihemoprotein ReductaseOxidation-ReductionProtein EngineeringPseudomonasRecombinant Fusion ProteinsBacterial ProteinsCytochrome P-450 Enzyme SystemEnzymesflavocytochrome P450 BM3 monoxygenasesFormate DehydrogenasesNADPNADPH-Ferrihemoprotein ReductaseRecombinant Fusion Proteins

Identifiers

PMID34737365
PMCPMC8568981

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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.