Evidence map›Paper›PMID 34467357›Full record

ArticleJACS Au2021

Substrate Channeling by a Rationally Designed Fusion Protein in a Biocatalytic Cascade.

Matthew J Kummer, Yoo Seok Lee, Mengwei Yuan, Bassam Alkotaini, John Zhao, Emmy Blumenthal, Shelley D Minteer

Abstract read
In one paragraph

Article in JACS Au, 2021. 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
–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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Activation-Free Upgrading of Carboxylic Acids to Aldehydes and Alcohols.bioRxiv : the preprint server for biology · 2025
    Article
  8. Leveraging EngineeredACS synthetic biology · 2025
    Article
  9. Article
  10. Article
  11. Advanced Electroanalysis for Electrosynthesis.ACS organic & inorganic Au · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Identification of vitamin BBiotechnology letters · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. 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.

Matthew J KummerDepartment of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, Utah 84112, United States.
Yoo Seok LeeDepartment of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, Utah 84112, United States.
Mengwei YuanDepartment of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, Utah 84112, United States.
Bassam AlkotainiDepartment of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, Utah 84112, United States.ORCID https://orcid.org/0000-0002-9924-6400
John ZhaoDepartment of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, Utah 84112, United States.
Emmy BlumenthalDepartment of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, Utah 84112, United States.
Shelley D MinteerDepartment of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, Utah 84112, United States.ORCID https://orcid.org/0000-0002-5788-2249

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COHEN, BRUCE E · 1985 to 2011
$17.6M
NCRR NIH HHS P41 RR001081
6 · The paper itself

Abstract

Substrate channeling, where an intermediate in a multistep reaction is directed toward a reaction center rather than freely diffusing, offers several advantages when employed in catalytic cascades. Here we present a fusion enzyme comprised of an alcohol and aldehyde dehydrogenase, that is computationally designed to facilitate electrostatic substrate channeling using a cationic linker bridging the two structures. Rosetta protein folding software was utilized to determine an optimal linker placement, added to the truncated termini of the proteins, which is as close as possible to the active sites of the enzymes without disrupting critical catalytic residues. With improvements in stability, product selectivity (90%), and catalyst turnover frequency, representing 500-fold increased activity compared to the unbound enzymes and nearly 140-fold for a neutral-linked fusion enzyme, this design strategy holds promise for making other multistep catalytic processes more sustainable and efficient.

Identifiers

PMID34467357
PMCPMC8397353

What OpenQuestion holds

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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.