Evidence map›Paper›PMID 36068220›Full record

ArticleNature communications2022

Substrate multiplexed protein engineering facilitates promiscuous biocatalytic synthesis.

Allwin D McDonald, Peyton M Higgins, Andrew R Buller

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Reconstituting a two-step pathway forMetabolic engineering communications · 2026
    Article
  2. Article
  3. Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Engineered Biocatalytic Synthesis of β-N-Substituted-α-Amino Acids.Angewandte Chemie (International ed. in English) · 2023
    Article
  14. Article
  15. Qualitative metabolomics-based characterization of a phenolic UDP-xylosyltransferase with a broad substrate spectrum fromProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. 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

3 authors.

Allwin D McDonald *Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0001-9559-0856
Peyton M Higgins *Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0001-5591-5046
Andrew R BullerDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA. arbuller@wisc.edu.ORCID http://orcid.org/0000-0002-9635-4844

Funding

Engineering in vivo biomolecular synthesis with non-standard building blocksDP2GM137417 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BULLER, ANDREW · 2019 to 2019
$2.2M
QExactive (Orbitrap) mass spectrometerS10OD020022 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI VESTLING, MARTHA M · 2015 to 2015
$483k
NIGMS NIH HHS DP2 GM137417NIH HHS S10 OD020022
6 · The paper itself

Abstract

Enzymes with high activity are readily produced through protein engineering, but intentionally and efficiently engineering enzymes for an expanded substrate scope is a contemporary challenge. One approach to address this challenge is Substrate Multiplexed Screening (SUMS), where enzyme activity is measured on competing substrates. SUMS has long been used to rigorously quantitate native enzyme specificity, primarily for in vivo settings. SUMS has more recently found sporadic use as a protein engineering approach but has not been widely adopted by the field, despite its potential utility. Here, we develop principles of how to design and interpret SUMS assays to guide protein engineering. This rich information enables improving activity with multiple substrates simultaneously, identifies enzyme variants with altered scope, and indicates potential mutational hot-spots as sites for further engineering. These advances leverage common laboratory equipment and represent a highly accessible and customizable method for enzyme engineering.

Indexed as

Protein EngineeringBiocatalysisSubstrate Specificity

Identifiers

PMID36068220
PMCPMC9448781

What OpenQuestion holds

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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.