Evidence map›Paper›PMID 42779916›Full record

ArticlebioRxiv : the preprint server for biology2026

High-throughput physics-based enzyme engineering.

Xujian Wang, Xiang Qiu, Yuyang Wu, Taoyu Niu, Shuhao Zhang, Runtian Gao, Ilkwon Cho, Haocheng Tang, Kangdelong Hu, Xiaoguang Lei and 2 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Xujian WangDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, United States.
Xiang QiuBeijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of the Ministry of Education, College of Chemistry and Molecular Engineering, New Cornerstone Science Laboratory, Peking University, Beijing, China.
Yuyang WuDepartment of Chemistry, Carnegie Mellon University, Pittsburgh,PA 15213, United States.
Taoyu NiuDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, United States.
Shuhao ZhangDepartment of Chemistry, Carnegie Mellon University, Pittsburgh,PA 15213, United States.
Runtian GaoDepartment of Chemistry, Carnegie Mellon University, Pittsburgh,PA 15213, United States.
Ilkwon ChoDepartment of Chemistry, Carnegie Mellon University, Pittsburgh,PA 15213, United States.
Haocheng TangDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, United States.
Kangdelong HuBeijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of the Ministry of Education, College of Chemistry and Molecular Engineering, New Cornerstone Science Laboratory, Peking University, Beijing, China.
Xiaoguang LeiBeijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of the Ministry of Education, College of Chemistry and Molecular Engineering, New Cornerstone Science Laboratory, Peking University, Beijing, China.
Olexandr IsayevDepartment of Chemistry, Carnegie Mellon University, Pittsburgh,PA 15213, United States.
Junmei WangDepartment of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, United States.

Funding

New Generation of General AMBER Force Field for Biomedical ResearchR01GM147673 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WANG, JUNMEI, YANG, WEI · 2022 to 2025
$1.5M
AI-Powered Biased Ligand DesignR01GM149705 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Junmei Wang · 2023 to 2026
$1.3M
NIGMS NIH HHS R01 GM147673NIGMS NIH HHS R01 GM149705
6 · The paper itself

Abstract

Enzyme engineering aims to tailor natural enzymes for industrial and therapeutic applications, yet physically grounded rational design has been limited by a trade-off between accuracy and cost, leaving the field heavily dependent on expert intuition. Here we present a scalable physics-based framework that combines field-aware machine learning with molecular mechanics to capture enzyme electrostatics at quantum-mechanical accuracy while enabling efficient, atomistic exploration of reaction free-energy landscapes. Coupled with microkinetic modelling, the framework translates molecular free-energy landscapes into catalytic rates and selectivity across competing, multistep reaction pathways. Applied to a newly engineered oxidative amidase (OxiAm), the framework predicts catalytic rate constants with near-experimental accuracy, quantitatively resolves the selectivity between hydrolysis and aminolysis, and generalizes across substrates, mutations and enzyme homologues. Transition-state ensemble analysis further reveals the reaction mechanism and guides the design of enzyme variants for pharmaceutical synthesis. By bringing chemical accuracy and high-throughput sampling to enzyme catalysis, this approach shifts rational design from static, empirical practice toward dynamic, free-energy-driven design, and should accelerate the engineering of biocatalysts.

Identifiers

PMID42779916
PMCPMC13596340

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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.