ArticleChem catalysis2025
SubTuner leverages physics-based modeling to complement AI in enzyme engineering toward non-native substrates.
Article in Chem catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Electrostatic Engineering of Phosphoketolase Enhances Activity on Small Nonphosphorylated Sugars and Improves Cell-Free ATP Regeneration from Inexpensive C2-Substrates.The journal of physical chemistry. B · 2026Article
- Artificial intelligence and automation in enzyme engineering: evolution, advances, and future perspectives.Bioresources and bioprocessing · 2026Review
- MutexaGPT: An Intuition-to-Design Translator for Physics-based Enzyme Engineering.Research square · 2026Article
- Sequence redesign of glycosyltransferases for enhanced heterologous expression and glycosylation efficiency in Escherichia coli.Nature communications · 2026Article
- Advances in Machine Learning Models for Predicting Enzyme Kinetic Parameters.Journal of chemical information and modeling · 2026Review
- Protein design drives synthetic biology research of plant natural products.Biodesign research · 2025Review
- Enzyme miniaturization: Revolutionizing future biocatalysts.Biotechnology advances · 2025Review
- Finding the dark matter: Large language model-based enzyme kinetic data extractor and its validation.Protein science : a publication of the Protein Society · 2025Article
- Linker-mediated domain separation enhances cold adaptation in cellulases.Protein science : a publication of the Protein Society · 2025Article
- Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.Angewandte Chemie (International ed. in English) · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
We developed SubTuner, a physics-based computational tool that tackles the challenge of identifying enzyme mutants with enhanced activity for specified non-native substrates. To test the performance of SubTuner, we designed three tasks - all aiming to identify beneficial anion methyltransferase mutants for synthesis of non-native S-adenosyl-l-methionine analogs: first in the conversion of ethyl iodide from a pool of 190 AtHOL1 single-point mutants for an initial test of accuracy and speed; second of ethyl, n-propyl, cyclopropylmethyl, and phenethyl iodide from a pool of 600 acl-MT multi-point mutants for a test of generalizability; and eventually of bulkier substrates for AtHOL1 combined with experimental characterization for a test of
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Registered trials
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