ArticleScientific reports2019
Pig liver esterases PLE1 and PLE6: heterologous expression, hydrolysis of common antibiotics and pharmacological consequences.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
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- Compared Inhibitory Activities of Tamoxifen and Avenanthramide B on Liver Esterase and Correlation Based on the Superimposed Structure Between Porcine and Human Liver Esterase.International journal of molecular sciences · 2024Article
- Chemical Composition of Seeds in Soybean Glycine soja (Fabaceae) of Amur Oblast.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2024Article
- Discovery, characterization and mechanism of a Microbacterium esterase for key d-biotin chiral intermediate synthesis.Bioresources and bioprocessing · 2024Article
- Selective and Concentrative Enteropancreatic Recirculation of Antibiotics by Pigs.Antibiotics (Basel, Switzerland) · 2023Article
- OMolecules (Basel, Switzerland) · 2022Article
- Ester Prodrugs of Malonate with Enhanced Intracellular Delivery Protect Against Cardiac Ischemia-Reperfusion Injury In Vivo.Cardiovascular drugs and therapy · 2022Article
- Pig Liver Esterases Hydrolyze Endocannabinoids and Promote Inflammatory Response.Frontiers in immunology · 2021Article
- Novel phenolic antimicrobials enhanced activity of iminodiacetate prodrugs against biofilm and planktonic bacteria.Chemical biology & drug design · 2021Article
- Selective Delivery of Dicarboxylates to Mitochondria by Conjugation to a Lipophilic Cation via a Cleavable Linker.Molecular pharmaceutics · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carboxylesterases, historically referred as non-specific esterases, are ubiquitous hydrolases with high catalytic efficiency. Without exceptions, all mammalian species studied contain multiple forms of carboxylesterases. While having been widely studied in humans and experimental animals, these enzymes remain to be characterized in farm animals. In this study, we showed that pig liver esterase 1 (PLE1) and pig liver esterase 6 (PLE6) were highly active toward amoxicillin (AMO) and ampicillin (AMP), two major antibiotics that are widely used in food-supplements. Mass-spectrometric analysis established that the hydrolysis occurred at the β-lactam amide bond and the hydrolysis drastically decreased or completely eliminated the antibacterial activity. Furthermore, hydrolytic activity and proteomic analysis suggested that trace PLEs existed in pig plasma and contributed little to the hydrolysis of AMO and AMP. These results suggested that carboxylesterases-based hydrolysis determines the therapeutic intensity of these and related antibiotics and the magnitude of the determination occurs in a species-dependent manner.
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