ArticleAngewandte Chemie (International ed. in English)2020
Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis.Nature communications · 2026Article
- 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
- Perspectives of aminoacylases in biocatalytic synthesis of N-acyl-amino acids surfactants.Applied microbiology and biotechnology · 2024Review
- Computational design of serine hydrolases.bioRxiv : the preprint server for biology · 2024Article
- Biocatalytic Heteroaromatic Amide Formation in Water Enabled by a Catalytic Tetrad and Two Access Tunnels.ACS catalysis · 2024Article
- Enhancing the Hydrolytic Activity of a Lipase towards Larger Triglycerides through Lid Domain Engineering.International journal of molecular sciences · 2023Article
- Sequence and Structural Motifs Controlling the Broad Substrate Specificity of the Mycobacterial Hormone-Sensitive Lipase LipN.ACS omega · 2023Article
- Enhancing the Hydrolysis and Acyl Transfer Activity of Carboxylesterase DLFae4 by a Combinational Mutagenesis and In-Silico Method.Foods (Basel, Switzerland) · 2023Article
- Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations.Biomolecules · 2023Article
- Alteration of Chain-Length Selectivity and Thermostability ofApplied and environmental microbiology · 2023Article
- Recovery of Hydroxytyrosol from Olive Mill Wastewater Using the Promiscuous Hydrolase/Acyltransferase PestE.Chembiochem : a European journal of chemical biology · 2022Article
- Carboxyl Methyltransferase Catalysed Formation of Mono- and Dimethyl Esters under Aqueous Conditions: Application in Cascade Biocatalysis.Angewandte Chemie (International ed. in English) · 2022Article
- Enzymatic synthesis of 2-phenethyl acetate in water catalyzed by an immobilized acyltransferase fromRSC advances · 2022Article
- Fatty Acids and their Derivatives as Renewable Platform Molecules for the Chemical Industry.Angewandte Chemie (International ed. in English) · 2021Review
- Rational Design for Enhanced Acyltransferase Activity in Water Catalyzed by theMicroorganisms · 2021Article
- Power of Biocatalysis for Organic Synthesis.ACS central science · 2021Review
- Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases.Angewandte Chemie (International ed. in English) · 2021Article
- Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family.Computational and structural biotechnology journal · 2021Article
- On the donor substrate dependence of group-transfer reactions by hydrolytic enzymes: Insight from kinetic analysis of sucrose phosphorylase-catalyzed transglycosylation.Biotechnology and bioengineering · 2020Article
- Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases.Angewandte Chemie (International ed. in English) · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Certain hydrolases preferentially catalyze acyl transfer over hydrolysis in an aqueous environment. However, the molecular and structural reasons for this phenomenon are still unclear. Herein, we provide evidence that acyltransferase activity in esterases highly correlates with the hydrophobicity of the substrate-binding pocket. A hydrophobicity scoring system developed in this work allows accurate prediction of promiscuous acyltransferase activity solely from the amino acid sequence of the cap domain. This concept was experimentally verified by systematic investigation of several homologous esterases, leading to the discovery of five novel promiscuous acyltransferases. We also developed a simple yet versatile colorimetric assay for rapid characterization of novel acyltransferases. This study demonstrates that promiscuous acyltransferase activity is not as rare as previously thought and provides access to a vast number of novel acyltransferases with diverse substrate specificity and potential applications.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.