Evidence map›Paper›PMID 33134840›Full record

ArticleNature catalysis2019

Elucidating structure-performance relationships in whole-cell cooperative enzyme catalysis.

Mason R Smith, Hui Gao, Ponnandy Prabhu, Luke F Bugada, Cori Roth, Deepika Mutukuri, Christine M Yee, Lester Lee, Robert M Ziff, Jung-Kul Lee and 1 more

Abstract read
In one paragraph

Article in Nature catalysis, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Synthetic and systems biotechnology · 2026
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  10. Review
  11. Characterization of Cellobiohydrolases fromIndian journal of microbiology · 2020
    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

11 authors.

Mason R SmithDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Hui GaoDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Ponnandy PrabhuDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Luke F BugadaDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Cori RothDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Deepika MutukuriDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Christine M YeeDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Lester LeeDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Robert M ZiffDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.
Jung-Kul LeeDepartment of Chemical Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Fei WenDepartment of Chemical Engineering, University of Michigan, Ann Arbor, Michigan 48109, United States.

Funding

Cytometry by Time of Fight (CyTOF) for High-speed Single-cell AnalysisS10OD020053 · OD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEN, FEI · 2016 to 2016
$600k
A la carte 2D artificial antigen presenting system mimicking supramolecular patterns in the natural immunological synapse for precise functional conditioning of tumor-specific T cellsR03CA191952 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEN, FEI · 2015 to 2016
$155k
NCI NIH HHS R03 CA191952NIH HHS S10 OD020053
6 · The paper itself

Abstract

Cooperative enzyme catalysis in nature has long inspired the application of engineered multi-enzyme assemblies for industrial biocatalysis. Despite considerable interest, efforts to harness the activity of cell-surface displayed multi-enzyme assemblies have been based on trial and error rather than rational design due to a lack of quantitative tools. In this study, we developed a quantitative approach to whole-cell biocatalyst characterization enabling a comprehensive study of how yeast-surface displayed multi-enzyme assemblies form. Here we show that the multi-enzyme assembly efficiency is limited by molecular crowding on the yeast cell surface, and that maximizing enzyme density is the most important parameter for enhancing cellulose hydrolytic performance. Interestingly, we also observed that proximity effects are only synergistic when the average inter-enzyme distance is > ~130 nm. The findings and the quantitative approach developed in this work should help to advance the field of biocatalyst engineering from trial and error to rational design.

Identifiers

PMID33134840
PMCPMC7597743

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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.