Evidence map›Paper›PMID 35084776›Full record

ArticleMicrobial biotechnology2022

Oligomerization engineering of the fluorinase enzyme leads to an active trimer that supports synthesis of fluorometabolites in vitro.

Tiia Kittilä, Patricia Calero, Folmer Fredslund, Phillip T Lowe, David Tezé, Manuel Nieto-Domínguez, David O'Hagan, Pablo I Nikel, Ditte H Welner

Open access · goldAbstract read
In one paragraph

Article in Microbial biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Synthetic metabolism forRSC chemical biology · 2022
    Article
  3. Article
  4. Article
  5. Identification of Two Novel Fluorinases FromFrontiers in bioengineering and biotechnology · 2022
    Article
  6. Biocatalytic synthesis of 2-fluoro-3-hydroxypropionic acid.Frontiers in bioengineering and biotechnology · 2022
    Article
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

9 authors at 2 institutions in 2 countries.

Tiia KittiläThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Patricia CaleroThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Folmer FredslundThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Phillip T LoweSchool of Chemistry, University of St. Andrews, St. Andrews, KY16 9ST, UK.
David TezéThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Manuel Nieto-DomínguezThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
David O'HaganSchool of Chemistry, University of St. Andrews, St. Andrews, KY16 9ST, UK.
Pablo I NikelThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.ORCID 0000-0002-9313-7481
Ditte H WelnerThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Novo Nordisk Foundation · DKUniversity of St Andrews · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fluorinase enzyme represents the only biological mechanism capable of forming stable C-F bonds characterized in nature thus far, offering a biotechnological route to the biosynthesis of value-added organofluorines. The fluorinase is known to operate in a hexameric form, but the consequence(s) of the oligomerization status on the enzyme activity and its catalytic properties remain largely unknown. In this work, this aspect was explored by rationally engineering trimeric fluorinase variants that retained the same catalytic rate as the wild-type enzyme. These results ruled out hexamerization as a requisite for the fluorination activity. The Michaelis constant (K

Indexed as

StreptomycesBacterial ProteinsMethionineOxidoreductasesS-AdenosylmethionineBacterial ProteinsfluorinaseMethionineOxidoreductasesS-Adenosylmethionine

Identifiers

PMID35084776
PMCPMC9049626
OpenAlexW4210675058

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.