ArticleSynthetic and systems biotechnology2024
Enhancing the activity and succinyl-CoA specificity of 3-ketoacyl-CoA thiolase Tfu_0875 through rational binding pocket engineering.
Article in Synthetic and systems biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 14 citations in OpenAlex.
- Artificial intelligence and automation in enzyme engineering: evolution, advances, and future perspectives.Bioresources and bioprocessing · 2026Review
- Combing Directed Enzyme Evolution with Metabolic Engineering to Develop Efficient Microbial Cell Factories.Chem & bio engineering · 2025Review
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5 authors at 1 institution in 1 country.
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Abstract
The 3-ketoacyl-CoA thiolase is the rate-limiting enzyme for linear dicarboxylic acids production. However, the promiscuous substrate specificity and suboptimal catalytic performance have restricted its application. Here we present both biochemical and structural analyses of a high-efficiency 3-ketoacyl-CoA thiolase Tfu_0875. Notably, Tfu_0875 displayed heightened activity and substrate specificity for succinyl-CoA, a key precursor in adipic acid production. To enhance its performance, a deep learning approach (DLKcat) was employed to identify effective mutants, and a computational strategy, known as the greedy accumulated strategy for protein engineering (GRAPE), was used to accumulate these effective mutants. Among the mutants, Tfu_0875
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