Evidence map›Paper›PMID 41816612›Full record

ArticleChemical science2026

Simulating enzyme catalysis with electrostatically embedded machine learning potentials.

Valentin Gradisteanu, Elliot W Chan, Lester Hedges, Meritxell Malagarriga, Rolf David, Miguel de la Puente, Damien Laage, Iñaki Tuñón, Marc W van der Kamp, Kirill Zinovjev

Abstract read
In one paragraph

Article in Chemical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

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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

10 authors.

Valentin GradisteanuDepartamento de Química Física, Universidad de Valencia 46100 Burjassot Spain kirill.zinovjev@uv.es.ORCID https://orcid.org/0009-0004-4923-6265
Elliot W ChanSchool of Biochemistry & Cellular and Molecular Medicine, University of Bristol Biomedical Sciences Building, University Walk Bristol BS8 1TD UK marc.vanderkamp@bristol.ac.uk.ORCID https://orcid.org/0000-0001-8807-8264
Lester HedgesSchool of Biochemistry & Cellular and Molecular Medicine, University of Bristol Biomedical Sciences Building, University Walk Bristol BS8 1TD UK marc.vanderkamp@bristol.ac.uk.ORCID https://orcid.org/0000-0002-5624-0500
Meritxell MalagarrigaDepartamento de Química Física, Universidad de Valencia 46100 Burjassot Spain kirill.zinovjev@uv.es.
Rolf DavidLaboratory CPCV, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne Université, CNRS Paris France.ORCID https://orcid.org/0000-0001-5338-6267
Miguel de la PuenteLaboratory CPCV, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne Université, CNRS Paris France.ORCID https://orcid.org/0000-0002-4432-9612
Damien LaageLaboratory CPCV, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne Université, CNRS Paris France.ORCID https://orcid.org/0000-0001-5706-9939
Iñaki TuñónDepartamento de Química Física, Universidad de Valencia 46100 Burjassot Spain kirill.zinovjev@uv.es.ORCID https://orcid.org/0000-0002-6995-1838
Marc W van der KampSchool of Biochemistry & Cellular and Molecular Medicine, University of Bristol Biomedical Sciences Building, University Walk Bristol BS8 1TD UK marc.vanderkamp@bristol.ac.uk.ORCID https://orcid.org/0000-0002-8060-3359
Kirill ZinovjevDepartamento de Química Física, Universidad de Valencia 46100 Burjassot Spain kirill.zinovjev@uv.es.ORCID https://orcid.org/0000-0003-1052-5698

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To simulate enzyme reactions, multiscale quantum mechanics/molecular mechanics (QM/MM) approaches are well established and popular. However, accurately and efficiently estimating enzyme activity is a challenge, because in general, precise methods are too computationally expensive. Here, we demonstrate that enzyme catalysis can be captured by coupling efficient, reactive machine-learned potentials (MLPs) trained on gas phase data to the wider enzyme environment using electrostatic machine learning embedding (EMLE). The EMLE scheme is first applied to the natural Diels-Alderase AbyU, showing that it correctly differentiates the catalytic action on different enzyme-substrate conformations. Then, we show that training a reaction-specific EMLE model allows us to accurately capture the enzyme catalytic effects of the conversion of chorismate to prephenate, a reaction with a highly polarizable and charged transition state. In both cases, in contrast to mechanical embedding approaches, the EMLE scheme allows accurate and efficient predictions of enzyme catalysis, agreeing with high-level QM/MM reference calculations. This approach facilitates the use of gas phase-trained MLPs in MLP/molecular mechanics (ML/MM) simulations and should thus be highly beneficial for computational activity screening of enzyme biocatalysts.

Identifiers

PMID41816612
PMCPMC12974892

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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.