Evidence map›Paper›PMID 25294646›Full record

ReviewJournal of applied microbiology2014

CYP105-diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces.

Suzy C Moody, E Joel Loveridge

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of applied microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. HApplied and environmental microbiology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. More P450s Are Involved in Secondary Metabolite Biosynthesis inInternational journal of molecular sciences · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  17. Article
  18. 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

2 authors at 2 institutions in 1 country.

Suzy C MoodyDepartment of Biosciences, College of Science, Swansea University, Swansea, UK.
E Joel Loveridge
Cardiff University · GBSwansea University · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

The cytochromes P450 (CYP or P450) are a large superfamily of haem-containing enzymes found in all domains of life. They catalyse a variety of complex reactions, predominantly mixed-function oxidations, often displaying highly regio- and/or stereospecific chemistry. In streptomycetes, they are predominantly associated with secondary metabolite biosynthetic pathways or with xenobiotic catabolism. Homologues of one family, CYP105, have been found in all Streptomyces species thus far sequenced. This review looks at the diverse biological functions of CYP105s and the biosynthetic/catabolic pathways they are associated with. Examples are presented showing a range of biotransformative abilities and different contexts. As biocatalysts capable of some remarkable chemistry, CYP105s have great biotechnological potential and merit detailed study. Recent developments in biotechnological applications which utilize CYP105s are described, alongside a brief overview of the benefits and drawbacks of using P450s in commercial applications. The role of CYP105s in vivo is in many cases undefined and provides a rich source for further investigation into the functions these enzymes fulfil and the metabolic pathways they participate in, in the natural environment.

Indexed as

Bacterial ProteinsCytochrome P-450 Enzyme SystemIndustrial MicrobiologyStreptomycesXenobioticsBacterial ProteinsCytochrome P-450 Enzyme SystemXenobioticsantimicrobialbioremediationbiotransformationP450polyketide synthesissecondary metabolismStreptomycesxenobiotic degradation

Identifiers

PMID25294646
PMCPMC4265290
OpenAlexW2163089754

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.