Evidence map›Paper›PMID 34815408›Full record

ArticleNature communications2021

Mapping enzyme catalysis with metabolic biosensing.

Linfeng Xu, Kai-Chun Chang, Emory M Payne, Cyrus Modavi, Leqian Liu, Claire M Palmer, Nannan Tao, Hal S Alper, Robert T Kennedy, Dale S Cornett and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. 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
1.8field-weighted citation impact, top 14% 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, 38 citations in OpenAlex.

  1. Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026
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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

11 authors at 4 institutions in 1 country.

Linfeng XuDepartment of Bioengineering and Therapeutic sciences, University of California, San Francisco, San Francisco, CA, USA.ORCID 0000-0002-6386-1815
Kai-Chun ChangDepartment of Bioengineering and Therapeutic sciences, University of California, San Francisco, San Francisco, CA, USA.
Emory M PayneDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA.ORCID 0000-0002-5956-8392
Cyrus ModaviDepartment of Bioengineering and Therapeutic sciences, University of California, San Francisco, San Francisco, CA, USA.
Leqian LiuDepartment of Bioengineering and Therapeutic sciences, University of California, San Francisco, San Francisco, CA, USA.
Claire M PalmerInstitute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-1581-159X
Nannan TaoBruker Nano Surfaces, San Jose, CA, USA.
Hal S AlperInstitute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-8246-8605
Robert T KennedyDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA.ORCID 0000-0003-2447-7471
Dale S CornettBruker Daltonics, Billerica, MA, USA.
Adam R AbateDepartment of Bioengineering and Therapeutic sciences, University of California, San Francisco, San Francisco, CA, USA. adam@abatelab.org.ORCID 0000-0001-9614-4831
University of California, San Francisco · USBruker (United States) · USThe University of Texas at Austin · USUniversity of Michigan · US

Funding

Gigapixel digital PCR in Giant Unilamellar VesiclesR01EB019453 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ABATE, ADAM R., CHIU, CHARLES YEN · 2014 to 2022
$3.9M
Microfluidics in Biomedical Sciences Training ProgramT32EB005582 · NIBIB · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FAN, XUDONG · 2005 to 2020
$3.9M
Accurate and unbiased single cell sequencing with digital droplet MDAR01HG008978 · NHGRI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ABATE, ADAM R. · 2016 to 2018
$1.9M
NHGRI NIH HHS R01 HG008978NIBIB NIH HHS R01 EB019453NIBIB NIH HHS T32 EB005582
6 · The paper itself

Abstract

Enzymes are represented across a vast space of protein sequences and structural forms and have activities that far exceed the best chemical catalysts; however, engineering them to have novel or enhanced activity is limited by technologies for sensing product formation. Here, we describe a general and scalable approach for characterizing enzyme activity that uses the metabolism of the host cell as a biosensor by which to infer product formation. Since different products consume different molecules in their synthesis, they perturb host metabolism in unique ways that can be measured by mass spectrometry. This provides a general way by which to sense product formation, to discover unexpected products and map the effects of mutagenesis.

Indexed as

Biosensing TechniquesAsteraceaeBiocatalysisEnzyme AssaysMetabolic EngineeringMicrofluidic Analytical TechniquesMutagenesisPlant ProteinsPolyketide SynthasesYarrowiaPlant ProteinsPolyketide Synthases

Identifiers

PMID34815408
PMCPMC8611028
OpenAlexW3215454153

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.