Evidence map›Paper›PMID 30341814›Full record

ArticleMicrobial biotechnology2019

Heterologous coexpression of the benzoate-para-hydroxylase CYP53B1 with different cytochrome P450 reductases in various yeasts.

Chrispian W Theron, Michel Labuschagné, Jacobus Albertyn, Martha S Smit

Open access · goldAbstract read
In one paragraph

Article in Microbial biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Nitroreduction of flutamide byBiochemistry and biophysics reports · 2022
    Article
  7. Article
  8. Construction and Optimization of theFrontiers in bioengineering and biotechnology · 2022
    Article
  9. Article
  10. Article
  11. 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

4 authors at 2 institutions in 1 country.

Chrispian W TheronDepartment of Microbial, Biochemical and Food Biotechnology, University of the Free State, Bloemfontein, South Africa.ORCID 0000-0002-8522-6417
Michel LabuschagnéDepartment of Microbial, Biochemical and Food Biotechnology, University of the Free State, Bloemfontein, South Africa.
Jacobus AlbertynDepartment of Microbial, Biochemical and Food Biotechnology, University of the Free State, Bloemfontein, South Africa.
Martha S SmitDepartment of Microbial, Biochemical and Food Biotechnology, University of the Free State, Bloemfontein, South Africa.ORCID 0000-0002-1295-6507
University of Cape Town · ZAUniversity of the Free State · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450 monooxygenases (P450) are enzymes with high potential as biocatalysts for industrial applications. Their large-scale applications are, however, limited by instability and requirement for coproteins and/or expensive cofactors. These problems are largely overcome when whole cells are used as biocatalysts. We previously screened various yeast species heterologously expressing self-sufficient P450s for their potential as whole-cell biocatalysts. Most P450s are, however, not self-sufficient and consist of two or three protein component systems. Therefore, in the present study, we screened different yeast species for coexpression of P450 and P450-reductase (CPR) partners, using CYP53B1 from Rhodotorula minuta as an exemplary P450. The abilities of three different coexpressed CPR partners to support P450 activity were investigated, two from basidiomycetous origin and one from an ascomycete. The various P450-CPR combinations were cloned into strains of Saccharomyces cerevisiae, Kluyveromyces marxianus, Hansenula polymorpha, Yarrowia lipolytica and Arxula adeninivorans, using a broad-range yeast expression vector. The results obtained supported the previous finding that recombinant A. adeninivorans strains perform excellently as whole-cell biocatalysts. This study also demonstrated for the first time the P450 reductase activity of the CPRs from R. minuta and U. maydis. A very interesting observation was the variation in the supportive activity provided by the different reductase partners tested and demonstrated better P450 activity enhancement by a heterologous CPR compared to its natural partner CPR. This study highlights reductase selection as a critical variable for consideration in the pursuit of optimal P450-based catalytic systems. The usefulness of A. adeninivorans as both a host for recombinant P450s and whole-cell biocatalyst was emphasized, supporting earlier findings.

Indexed as

Gene ExpressionBenzoate 4-MonooxygenaseBenzoic AcidBiotransformationCloning, MolecularFungal ProteinsOxidoreductasesRecombinant ProteinsTransformation, GeneticYeastsBenzoate 4-MonooxygenaseBenzoic AcidFungal ProteinsOxidoreductasesRecombinant Proteins

Identifiers

PMID30341814
PMCPMC6801163
OpenAlexW2898003828

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.