Evidence map›Paper›PMID 28109855›Full record

ArticleProtein expression and purification2017

Heterologous expression and characterization of plant Taxadiene-5α-Hydroxylase (CYP725A4) in Escherichia coli.

John Edward Rouck, Bradley Walters Biggs, Amogh Kambalyal, William R Arnold, Marjan De Mey, Parayil Kumaran Ajikumar, Aditi Das

Open access · greenAbstract read
In one paragraph

Article in Protein expression and purification, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  4. Way to efficient microbial paclitaxel mass production.Synthetic and systems biotechnology · 2023
    Review
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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

7 authors at 4 institutions in 2 countries.

John Edward RouckDepartment of Comparative Biosciences, Department of Biochemistry, Department of Bioengineering, Division of Nutritional Science, Center for Biophysics and Quantitative Biology, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA.
Bradley Walters BiggsManus Biosynthesis, 1030 Massachusetts Avenue, Suite 300, Cambridge, MA 02138, USA; Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL 60208, USA.
Amogh KambalyalDepartment of Comparative Biosciences, Department of Biochemistry, Department of Bioengineering, Division of Nutritional Science, Center for Biophysics and Quantitative Biology, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA.
William R ArnoldDepartment of Comparative Biosciences, Department of Biochemistry, Department of Bioengineering, Division of Nutritional Science, Center for Biophysics and Quantitative Biology, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA.
Marjan De MeyCentre for Industrial Biotechnology and Biocatalysis, Ghent University, Coupure Links 653, B-9000, Belgium.
Parayil Kumaran AjikumarManus Biosynthesis, 1030 Massachusetts Avenue, Suite 300, Cambridge, MA 02138, USA. Electronic address: pkaji@manusbio.com.
Aditi DasDepartment of Comparative Biosciences, Department of Biochemistry, Department of Bioengineering, Division of Nutritional Science, Center for Biophysics and Quantitative Biology, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: aditidas@illinois.edu.
University of Illinois Urbana-Champaign · USGhent University · BEManus Bio (United States) · USNorthwestern University · US

Funding

Biochemical Mechanism of Eicosanoid Synthesizing EnzymesR01GM115584 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI DAS, ADITI · 2017 to 2022
$1.7M
NIGMS NIH HHS R01 GM115584
6 · The paper itself

Abstract

Taxadiene-5α-Hydroxylase (CYP725A4) is a membrane-bound plant cytochrome P450 that catalyzes the oxidation of taxadiene to taxadiene-5α-ol. This oxidation is a key step in the production of the valuable cancer therapeutic and natural plant product, taxol. In this work, we report the bacterial expression and purification of six different constructs of CYP725A4. All six of these constructs are N-terminally modified and three of them are fused to cytochrome P450 reductase to form a chimera construct. The construct with the highest yield of CYP725A4 protein was then selected for substrate binding and kinetic analysis. Taxadiene binding followed type-1 substrate patterns with an observed K

Indexed as

Cytochrome P-450 Enzyme SystemPlant ProteinsAlkenesBinding SitesDiterpenesEscherichia coliKineticsRecombinant ProteinsTaxusAlkenesCytochrome P-450 Enzyme SystemDiterpenesPlant ProteinsRecombinant Proteinstaxa-4(5),11(12)dieneE. coliNanodiscsRecombinant expressionTaxadieneTaxadiene-5α-ol

Identifiers

PMID28109855
PMCPMC5741078
OpenAlexW2575851676

What OpenQuestion holds

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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.