ArticleAngewandte Chemie (International ed. in English)2021
Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 45 citations in OpenAlex.
- Expression, purification, and in vitro characterization of the carboxylesterase CEST-9.2 from Caenorhabditis elegans.Bioscience reports · 2026Article
- Amide and Thioester Synthesis Via Oxidative Coupling of Alcohols with Amines or Thiols Using Alcohol Dehydrogenases.Angewandte Chemie (International ed. in English) · 2026Article
- Discovery and characterization of an enantioselective family VIII esterase from effluent treatment plant sludge metagenome.Scientific reports · 2025Article
- One-Pot Depolymerization of Mixed Plastics Using a Dual Enzyme System.ChemSusChem · 2025Article
- Development of the Esterase PestE for Amide Bond Synthesis Under Aqueous Conditions: Enzyme Cascades for Converting Waste PET into Tamibarotene.Angewandte Chemie (International ed. in English) · 2025Article
- Biocatalytic Heteroaromatic Amide Formation in Water Enabled by a Catalytic Tetrad and Two Access Tunnels.ACS catalysis · 2024Article
- Broad Spectrum Enantioselective Amide Bond Synthetase fromACS catalysis · 2024Article
- Enhancing the Hydrolysis and Acyl Transfer Activity of Carboxylesterase DLFae4 by a Combinational Mutagenesis and In-Silico Method.Foods (Basel, Switzerland) · 2023Article
- Genome-wide analysis of lipolytic enzymes and characterization of a high-tolerant carboxylesterase fromFrontiers in microbiology · 2023Article
- Crystal structure of a family VIII β-lactamase fold hydrolase reveals the molecular mechanism for its broad substrate scope.The FEBS journal · 2022Article
- A Plurizyme with Transaminase and Hydrolase Activity Catalyzes Cascade Reactions.Angewandte Chemie (International ed. in English) · 2022Article
- Identification and characterization of a novel carboxylesterase EstQ7 from a soil metagenomic library.Archives of microbiology · 2021Article
- Rational Design for Enhanced Acyltransferase Activity in Water Catalyzed by theMicroorganisms · 2021Article
- Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases.Angewandte Chemie (International ed. in English) · 2021Article
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8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Promiscuous acyltransferase activity is the ability of certain hydrolases to preferentially catalyze acyl transfer over hydrolysis, even in bulk water. However, poor enantioselectivity, low transfer efficiency, significant product hydrolysis, and limited substrate scope represent considerable drawbacks for their application. By activity-based screening of several hydrolases, we identified the family VIII carboxylesterase, EstCE1, as an unprecedentedly efficient acyltransferase. EstCE1 catalyzes the irreversible amidation and carbamoylation of amines in water, which enabled the synthesis of the drug moclobemide from methyl 4-chlorobenzoate and 4-(2-aminoethyl)morpholine (ca. 20 % conversion). We solved the crystal structure of EstCE1 and detailed structure-function analysis revealed a three-amino acid motif important for promiscuous acyltransferase activity. Introducing this motif into an esterase without acetyltransferase activity transformed a "hydrolase" into an "acyltransferase".
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