Evidence map›Paper›PMID 30119014›Full record

ArticleJournal of inorganic biochemistry2018

Structural and catalytic properties of the peroxygenase P450 enzyme CYP152K6 from Bacillus methanolicus.

Hazel M Girvan, Harshwardhan Poddar, Kirsty J McLean, David R Nelson, Katherine A Hollywood, Colin W Levy, David Leys, Andrew W Munro

Open access · hybridAbstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Recent Progress on Peroxidase Modification and Application.Applied biochemistry and biotechnology · 2024
    Review
  4. Design of a HProtein science : a publication of the Protein Society · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. 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

8 authors at 2 institutions in 2 countries.

Hazel M GirvanCentre for Synthetic Biology of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester M1 7DN, United Kingdom.
Harshwardhan PoddarCentre for Synthetic Biology of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester M1 7DN, United Kingdom.
Kirsty J McLeanCentre for Synthetic Biology of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester M1 7DN, United Kingdom.
David R NelsonDepartment of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, TN 38163, United States of America.
Katherine A HollywoodCentre for Synthetic Biology of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester M1 7DN, United Kingdom.
Colin W LevyCentre for Synthetic Biology of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester M1 7DN, United Kingdom.
David LeysCentre for Synthetic Biology of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester M1 7DN, United Kingdom.
Andrew W MunroCentre for Synthetic Biology of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester M1 7DN, United Kingdom. Electronic address: Andrew.Munro@Manchester.ac.uk.
University of Manchester · GBUniversity of Tennessee Health Science Center · US

Funding

Biotechnology and Biological Sciences Research Council BB/K017802/1Biotechnology and Biological Sciences Research Council BB/M017702/1Biotechnology and Biological Sciences Research Council BB/P000622/1
6 · The paper itself

Abstract

The CYP152 family of cytochrome P450 enzymes (P450s or CYPs) are bacterial peroxygenases that use hydrogen peroxide to drive hydroxylation and decarboxylation of fatty acid substrates. We have expressed and purified a novel CYP152 family member - CYP152K6 from the methylotroph Bacillus methanolicus MGA3. CYP152K6 was characterized using spectroscopic, analytical and structural methods. CYP152K6, like its peroxygenase counterpart P450

Indexed as

BacillusBacterial ProteinsCatalysisCatalytic DomainCrystallography, X-RayCytochrome P-450 Enzyme SystemFatty AcidsHydroxylationSubstrate SpecificityBacterial ProteinsCytochrome P-450 Enzyme SystemFatty AcidsCytochrome P450EPR spectroscopyOrganic productsPeroxygenaseProtein structureSubstrate binding

Identifiers

PMID30119014
PMCPMC6167049
OpenAlexW2886684370

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.