Evidence map›Paper›PMID 31140688›Full record

ArticleAngewandte Chemie (International ed. in English)2019

A High-Throughput Mass Spectrometric Enzyme Activity Assay Enabling the Discovery of Cytochrome P450 Biocatalysts.

Tristan de Rond, Jian Gao, Amin Zargar, Markus de Raad, Jack Cunha, Trent R Northen, Jay D Keasling

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. A novel P450 enzyme assay utilizing an NADPBiotechnology letters · 2025
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. A roadmap for metagenomic enzyme discovery.Natural product reports · 2021
    Review
  8. Review
  9. Article
  10. Perfluorocarbons in Chemical Biology.Chembiochem : a European journal of chemical biology · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. 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

7 authors.

Tristan de RondCollege of Chemistry, University of California, Berkeley, Berkeley, CA, 94270, USA.ORCID 0000-0002-5203-4662
Jian GaoDepartment of Energy Joint Genome Institute (DOE JGI), Lawrence Berkeley National Laboratory, USA.
Amin ZargarJoint Bioenergy Institute (JBEI), Lawrence Berkeley National Laboratory, Emeryville, CA, 94608, USA.
Markus de RaadDepartment of Energy Joint Genome Institute (DOE JGI), Lawrence Berkeley National Laboratory, USA.ORCID 0000-0001-8263-9198
Jack CunhaJoint Bioenergy Institute (JBEI), Lawrence Berkeley National Laboratory, Emeryville, CA, 94608, USA.
Trent R NorthenJoint Bioenergy Institute (JBEI), Lawrence Berkeley National Laboratory, Emeryville, CA, 94608, USA.ORCID 0000-0001-8404-3259
Jay D KeaslingCollege of Chemistry, University of California, Berkeley, Berkeley, CA, 94270, USA.ORCID 0000-0003-4170-6088

Funding

Enzyme-Mediated Synthesis of Functionalized Terpene StructuresRC1GM090980 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KEASLING, JAY D · 2009 to 2010
$1.0M
Elucidating the genetic basis of imidazopyrazinone luciferin biosynthesis for the development of improved bioluminescence imaging technologiesF32GM129960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DE ROND, TRISTAN · 2018 to 2020
$185k
Generating an Actinobacterial Chassis for Antimicrobial DiscoveryF32GM125179 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZARGAR, AMIN · 2018 to 2020
$146k
Biological and Environmental Research DE-AC02-05CH11231Directorate for Biological Sciences 1341894Directorate for Biological Sciences 1442724NIGMS NIH HHS F32 GM125179NIGMS NIH HHS F32 GM129960NIGMS NIH HHS RC1 GM090980
6 · The paper itself

Abstract

Assaying for enzymatic activity is a persistent bottleneck in biocatalyst and drug development. Existing high-throughput assays for enzyme activity tend to be applicable only to a narrow range of biochemical transformations, whereas universal enzyme characterization methods usually require chromatography to determine substrate turnover, greatly diminishing throughput. We present an enzyme activity assay that allows the high-throughput mass-spectrometric detection of enzyme activity in complex matrices without the need for a chromatographic step. This technology, which we call probing enzymes with click-assisted NIMS (PECAN), can detect the activity of medically and biocatalytically significant cytochrome P450s in cell lysate, microsomes, and bacteria. Using this approach, a cytochrome P450

Indexed as

Biological AssayCatalysisCytochrome P-450 Enzyme SystemDrug DevelopmentHigh-Throughput Screening AssaysMass SpectrometrySubstrate SpecificityCytochrome P-450 Enzyme Systembiocatalysiscytochrome P450enzyme assayshigh-throughput screeningmass spectrometry

Identifiers

PMID31140688
PMCPMC6640108

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Registered trials

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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.