ArticleComputational and structural biotechnology journal2021
Evolutionary coupling-inspired engineering of alcohol dehydrogenase reveals the influence of distant sites on its catalytic efficiency for stereospecific synthesis of chiral alcohols.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Engineering a Novel Cofactor-Versatile Short-Chain Dehydrogenase for Efficient Synthesis of Chiral Alcohols.Biotechnology and bioengineering · 2026Article
- Article
- Metabolic engineering of Saccharomyces cerevisiae for high-level production of (+)-ambrein from glucose.Biotechnology letters · 2024Article
- Thermal Stability Enhancement of L-Asparaginase fromFoods (Basel, Switzerland) · 2023Article
- Enhancing the Catalytic Activity of Type II L-Asparaginase fromInternational journal of molecular sciences · 2022Article
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10 authors.
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Abstract
Alcohol dehydrogenase (ADH) has attracted much attention due to its ability to catalyze the synthesis of important chiral alcohol pharmaceutical intermediates with high stereoselectivity. ADH protein engineering efforts have generally focused on reshaping the substrate-binding pocket. However, distant sites outside the pocket may also affect its activity, although the underlying molecular mechanism remains unclear. The current study aimed to apply evolutionary coupling-inspired engineering to the ADH CpRCR and to identify potential mutation sites. Through conservative analysis, phylogenic analysis and residues distribution analysis, the co-evolution hotspots Leu34 and Leu137 were confirmed to be highly evolved under the pressure of natural selection and to be possibly related to the catalytic function of the protein. Hence, Leu34 and Leu137, far away from the active center, were selected for mutation. The generated CpRCR-L34A and CpRCR-L137V variants showed high stereoselectivity and 1.24-7.81 fold increase in
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