Evidence map›Paper›PMID 32557882›Full record

ReviewProtein science : a publication of the Protein Society2020

A mechanistic view of enzyme evolution.

Gloria Yang, Charlotte M Miton, Nobuhiko Tokuriki

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Review
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  10. iScience · 2025
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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

3 authors.

Gloria YangMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada.ORCID 0000-0002-9139-6148
Charlotte M MitonMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada.ORCID 0000-0002-2374-303X
Nobuhiko TokurikiMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada.ORCID 0000-0002-8235-1829

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

New enzyme functions often evolve through the recruitment and optimization of latent promiscuous activities. How do mutations alter the molecular architecture of enzymes to enhance their activities? Can we infer general mechanisms that are common to most enzymes, or does each enzyme require a unique optimization process? The ability to predict the location and type of mutations necessary to enhance an enzyme's activity is critical to protein engineering and rational design. In this review, via the detailed examination of recent studies that have shed new light on the molecular changes underlying the optimization of enzyme function, we provide a mechanistic perspective of enzyme evolution. We first present a global survey of the prevalence of activity-enhancing mutations and their distribution within protein structures. We then delve into the molecular solutions that mediate functional optimization, specifically highlighting several common mechanisms that have been observed across multiple examples. As distinct protein sequences encounter different evolutionary bottlenecks, different mechanisms are likely to emerge along evolutionary trajectories toward improved function. Identifying the specific mechanism(s) that need to be improved upon, and tailoring our engineering efforts to each sequence, may considerably improve our chances to succeed in generating highly efficient catalysts in the future.

Indexed as

Directed Molecular EvolutionEnzymesEvolution, MolecularProtein EngineeringProtein DomainsSubstrate SpecificityEnzymesactivity-enhancing mutationsancestral sequence reconstructionconformational dynamicsconformational tinkeringdirected evolutionenzyme evolutionenzyme promiscuityenzyme-substrate complementaritymolecular mechanismssubstrate repositioning

Identifiers

PMID32557882
PMCPMC7380680

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.