ArticleAnalytical chemistry2019
Terbium(III) Luminescence-Based Assay for Esterase Activity.
Article in Analytical chemistry, 2019. 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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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.
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Who cites it
5 citing papers in PubMed.
- Luminescent Lanthanides in Biorelated Applications: From Molecules to Nanoparticles and Diagnostic Probes to Therapeutics.Chemical reviews · 2025Review
- Mammalian Esterase Activity: Implications for Peptide Prodrugs.Biochemistry · 2024Article
- New Advances in the Exploration of Esterases with PET and Fluorescent Probes.Molecules (Basel, Switzerland) · 2023Review
- Assessing and utilizing esterase specificity in antimicrobial prodrug development.Methods in enzymology · 2022Article
- Endogenous Enzymes Enable Antimicrobial Activity.ACS chemical biology · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Esterases catalyze the hydrolysis of esters to form a carboxylic acid and alcohol. These enzymes play a key role in both the detoxification of xenobiotic compounds and the metabolism of drugs and prodrugs. Numerous fluorogenic probes have been developed to monitor esterase activity. Most are based on an aromatic alcohol, and the others are based on an aromatic acid. These restrictions leave unexplored the specificity of esterases for aliphatic esters. Here, we report on the use of esters of thiopheneacetic acid coupled with the luminescence of terbium(III) as the basis for a continuous assay of esterase activity. This probe allows for a wide variation of the alcohol moiety and the detection of its hydrolysis at submicromolar concentrations. The assay verifies steady-state kinetic parameters for catalysis by pig liver esterase from either initial rates or the integration of progress curves, and its utility is evident with unpurified esterases in bacterial and human cell lysates.
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Registered trials
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