Evidence map›Paper›PMID 35333425›Full record

ArticleChembiochem : a European journal of chemical biology2022

Artificial Fusions between P450 BM3 and an Alcohol Dehydrogenase for Efficient (+)-Nootkatone Production.

Arsenij Kokorin, Vlada B Urlacher

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

3 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

2 authors at 1 institution in 1 country.

Arsenij KokorinInstitute of Biochemistry, Heinrich-Heine University Düsseldorf, Universitätsstrasse 1, Düsseldorf, 40225, Germany.
Vlada B UrlacherInstitute of Biochemistry, Heinrich-Heine University Düsseldorf, Universitätsstrasse 1, Düsseldorf, 40225, Germany.ORCID 0000-0003-1312-4574
Heinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multi-enzyme cascades enable the production of valuable chemical compounds, and fusion of the enzymes that catalyze these reactions can improve the reaction outcome. In this work, P450 BM3 from Bacillus megaterium and an alcohol dehydrogenase from Sphingomonas yanoikuyae were fused to bifunctional constructs to enable cofactor regeneration and improve the in vitro two-step oxidation of (+)-valencene to (+)-nootkatone. An up to 1.5-fold increased activity of P450 BM3 was achieved with the fusion constructs compared to the individual enzyme. Conversion of (+)-valencene coupled to cofactor regeneration and performed in the presence of the solubilizing agent cyclodextrin resulted in up to 1080 mg L

Indexed as

Alcohol DehydrogenaseBacillus megateriumBacterial ProteinsCytochrome P-450 Enzyme SystemNADPH-Ferrihemoprotein ReductasePolycyclic SesquiterpenesAlcohol DehydrogenaseBacterial ProteinsCytochrome P-450 Enzyme SystemNADPH-Ferrihemoprotein ReductasenootkatonePolycyclic Sesquiterpenesalcohol dehydrogenasesbiocatalysiscyclodextrinscytochrome P450enzyme fusion(+)-nootkatone

Identifiers

PMID35333425
PMCPMC9325546
OpenAlexW4220768656

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.