EP-Pred: A Machine Learning Tool for Bioprospecting Promiscuous Ester Hydrolases
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Abstract
When bioprospecting for novel industrial enzymes, substrate promiscuity is a desirable property that increases the reusability of the enzyme. Among industrial enzymes, ester hydrolases have great relevance for which the demand has not ceased to increase. However, the search for new substrate promiscuous ester hydrolases is not trivial since the mechanism behind this property is greatly influenced by the active site’s structural and physicochemical characteristics. These characteristics must be computed from the 3D structure, which is rarely available and expensive to measure, hence the need for a method that can predict promiscuity from sequence alone. Here we report such a method called EP-pred, an ensemble binary classifier, that combines three machine learning algorithms: SVM, KNN, and a Linear model. EP-pred has been evaluated against the Lipase Engineering Database together with a hidden Markov approach leading to a final set of ten sequences predicted to encode promiscuous esterases. Experimental results confirmed the validity of our method since all ten proteins were found to exhibit a broad substrate ambiguity.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Deep learning-based kcat prediction enables improved enzyme-constrained model reconstruction
Li, F., Yuan, L., Lu, H., Li, G., Chen, Y., Engqvist, M. K. M., Kerkhoven, E. J., & Nielsen, J. (2022) · Nature Catalysis · doi:10.1038/s41929-022-00798-z · Cited by 466 · see citing works
Machine learning modeling of family wide enzyme-substrate specificity screens
Goldman, S., Das, R., Yang, K. K., & Coley, C. W. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009853 · Cited by 120 · see citing works
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- Authors
- Xiang, R., Fernandez-Lopez, L., Robles-Martín, A., Ferrer, M., & Guallar, V.
- Affiliations
- Barcelona Supercomputing Center (ES)
- Department of Applied Biocatalysis, ICP, CSIC, 28049 Madrid, Spain
- Department of Life Sciences, Barcelona Supercomputing Center (BSC), 08034 Barcelona, Spain
- Consejo Superior de Investigaciones Científicas (ES)
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2022-10-21
- Volume
- 12
- Issue
- 10
- Pages
- 1529
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC9599548
- OpenAlex
- W4307122022
- Cited by
- 9
- References
- 3
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 1 · 2023: 2
- FWCI
- 0.41
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UPCommons institutional repository (Universitat Politècnica de Catalunya) (submittedVersion, cc-by-nc-nd)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- European Union (101000327, 101000607)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- ester hydrolase, substrate promiscuity, lipase, industrial enzymes
- MeSH terms
- Machine Learning, Esterases, Esters, Lipase, Bioprospecting
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