ArticleArchives of biochemistry and biophysics2016
Interaction of the serine hydrolase KIAA1363 with organophosphorus agents: Evaluation of potency and kinetics.
Article in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Characterization of an Arginine Decarboxylase fromBiomolecules · 2024Article
- KIAA1363-A Multifunctional Enzyme in Xenobiotic Detoxification and Lipid Ester Hydrolysis.Metabolites · 2022Review
- KIAA1363 affects retinyl ester turnover in cultured murine and human hepatic stellate cells.Journal of lipid research · 2022Article
- NAD(P)-dependent steroid dehydrogenase-like protein and neutral cholesterol ester hydrolase 1 serve as novel markers for early detection of gastric cancer identified using quantitative proteomics.Journal of clinical laboratory analysis · 2021Article
- Functional Omics Identifies Serine Hydrolases That Mobilize Storage Lipids during Rice Seed Germination.Plant physiology · 2020Article
- Activity-based protein profiling of rice (Oryza sativa L.) bran serine hydrolases.Scientific reports · 2020Article
- Structure Dependent Determination of Organophosphate Targets in Mammalian Tissues Using Activity-Based Protein Profiling.Chemical research in toxicology · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Oxons are bioactive metabolites of organophosphorus insecticides (OPs) that covalently inactivate serine hydrolases. KIAA1363 is one of the most abundant serine hydrolases in mouse brain. Although the physiological consequences related to the inhibition of KIAA1363 due to environmental exposures to OPs are poorly understood, the enzyme was previously shown to have a role in the detoxification of oxons. Here, we overexpressed human KIAA1363 and CES1 in COS7 cells and compared the potency of inhibition (IC50s, 15 min) of KIAA1363 and CES1 by chlorpyrifos oxon (CPO), paraoxon (PO), and methyl paraoxon (MPO). The order of potency was CPO > PO >> MPO for both enzymes. We also determined the bimolecular rate constants (kinact/Ki) for reactions of CPO and PO with KIAA1363 and CES1. KIAA1363 and CES1 were inactivated by CPO at comparable rates (4.4 × 10(6) s(-1) M(-1) and 6.7 × 10(6) s(-1) M(-1), respectively), whereas PO inactivated both enzymes at slower rates (0.4 × 10(6) s(-1) M(-1) and 1.5 × 10(6) s(-1) M(-1), respectively). Finally, the reactivation rate of KIAA1363 following inhibition by CPO was evaluated. Together, the results define the kinetics of inhibition of KIAA1363 by active metabolites of agrochemicals and indicate that KIAA1363 is highly sensitive to inhibition by these compounds.
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