Evidence map›Paper›PMID 26838175›Full record

ArticleMicrobial cell factories2016

Co-expression of active human cytochrome P450 1A2 and cytochrome P450 reductase on the cell surface of Escherichia coli.

Paul Quehl, Joel Hollender, Jan Schüürmann, Tatjana Brossette, Ruth Maas, Joachim Jose

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.7field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 57 citations in OpenAlex.

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  10. Bioconversion of vitamin DBiotechnology for biofuels and bioproducts · 2022
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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

6 authors at 1 institution in 1 country.

Paul QuehlInstitut für Pharmazeutische und Medizinische Chemie, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstraße 48, 48149, Münster, Germany. paul.quehl@uni-muenster.de.
Joel HollenderInstitut für Pharmazeutische und Medizinische Chemie, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstraße 48, 48149, Münster, Germany. mail.hollender@gmail.com.
Jan SchüürmannInstitut für Pharmazeutische und Medizinische Chemie, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstraße 48, 48149, Münster, Germany. jan.schueuermann@uni-muenster.de.
Tatjana BrossetteAutodisplay Biotech GmbH, Merowingerplatz 1a, 40225, Düsseldorf, Germany. tatjana.brossette@autodisplay-biotech.com.
Ruth MaasAutodisplay Biotech GmbH, Merowingerplatz 1a, 40225, Düsseldorf, Germany. ruth.maas@autodisplay-biotech.com.
Joachim JoseInstitut für Pharmazeutische und Medizinische Chemie, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstraße 48, 48149, Münster, Germany. joachim.jose@uni-muenster.de.
University of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHuman cytochrome P450 (CYP) enzymes mediate the first step in the breakdown of most drugs and are strongly involved in drug-drug interactions, drug clearance and activation of prodrugs. Their biocatalytic behavior is a key parameter during drug development which requires preparative synthesis of CYP related drug metabolites. However, recombinant expression of CYP enzymes is a challenging bottleneck for drug metabolite biosynthesis. Therefore, we developed a novel approach by displaying human cytochrome P450 1A2 (CYP1A2) and cytochrome P450 reductase (CPR) on the surface of Escherichia coli.

resultsTo present human CYP1A2 and CPR on the surface, we employed autodisplay. Both enzymes were displayed on the surface which was demonstrated by protease and antibody accessibility tests. CPR activity was first confirmed with the protein substrate cytochrome c. Cells co-expressing CYP1A2 and CPR were capable of catalyzing the conversion of the known CYP1A2 substrates 7-ethoxyresorufin, phenacetin and the artificial substrate luciferin-MultiCYP, which would not have been possible without interaction of both enzymes. Biocatalytic activity was strongly influenced by the composition of the growth medium. Addition of 5-aminolevulinic acid was necessary to obtain a fully active whole cell biocatalyst and was superior to the addition of heme.

conclusionWe demonstrated that CYP1A2 and CPR can be co-expressed catalytically active on the cell surface of E. coli. It is a promising step towards pharmaceutical applications such as the synthesis of drug metabolites.

Indexed as

Gene ExpressionBase SequenceBiocatalysisCell MembraneCulture MediaCytochrome P-450 CYP1A2Cytochromes cEscherichia coliFlow CytometryFluorescent Antibody TechniqueGenetic VectorsHumansMolecular Sequence DataOxazinesPeptide HydrolasesPhenacetinCulture MediaCYP1A2 protein, humanCytochrome P-450 CYP1A2Cytochromes cethoxyresorufinOxazinesPeptide HydrolasesPhenacetin

Identifiers

PMID26838175
PMCPMC4736170
OpenAlexW2266533396

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.