ArticleThe Journal of organic chemistry2021
Tunable Artificial Enzyme-Cofactor Complex for Selective Hydrolysis of Acetals.
Article in The Journal of organic chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Supramolecular Regulation of Catalytic Activity in Molecularly Responsive Catalysts.The Journal of organic chemistry · 2023Article
- Dynamic Tuning in Synthetic Glycosidase for Selective Hydrolysis of Alkyl and Aryl Glycosides.The Journal of organic chemistry · 2022Article
- Substrate Protection in Controlled Enzymatic Transformation of Peptides and Proteins.Chembiochem : a European journal of chemical biology · 2021Article
- Tandem Aldol Reaction from Acetal Mixtures by an Artificial Enzyme with Site-Isolated Acid and Base Functionalities.ACS applied polymer materials · 2021Article
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Authors and funding
3 authors.
Funding
Abstract
Enzymes frequently use unimpressive functional groups such as weak carboxylic acids for efficient, highly selective catalysis including hydrolysis of acetals and even amides. Much stronger acids generally have to be used for such purposes in synthetic systems. We report here a method to position an acidic group near the acetal oxygen of 2-(4-nitrophenyl)-1,3-dioxolane bound by an artificial enzyme. The hydrolytic activity of the resulting artificial enzyme-cofactor complex was tuned by the number and depth of the active site as well as the hydrophobicity and acidity of the cofactor. The selectivity of the complex was controlled by the size and shape of the active site and enabled less reactive acetals to be hydrolyzed over more reactive ones.
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