ArticleJournal of molecular biology2006
Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 141 citations in OpenAlex.
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- Expression, purification, and in vitro characterization of the carboxylesterase CEST-9.2 from Caenorhabditis elegans.Bioscience reports · 2026Article
- Experimental and In Silico Approaches to Study Carboxylesterase Substrate Specificity.Journal of xenobiotics · 2026Review
- Triazine Thiols Decrease Apolipoprotein B Secretion From Hepatocytes Through Inhibition of Human Carboxylesterase 1.Cellular and molecular gastroenterology and hepatology · 2026Article
- Synthesis and anticancer potential of glycosides.RSC advances · 2025Review
- Dimethyl Fumarate vs. Monomethyl Fumarate: Unresolved Pharmacologic Issues.Pharmaceutics · 2025Review
- Fluorogenic chemical tools to shed light on CES1-mediated adverse drug interactions.Chemical communications (Cambridge, England) · 2024Article
- Modeling onActa pharmaceutica Sinica. B · 2024Article
- Identification of flucloxacillin-modified hepatocellular proteins: implications in flucloxacillin-induced liver injury.Toxicological sciences : an official journal of the Society of Toxicology · 2023Article
- Characterisation of AMB-FUBINACA metabolism and CBForensic toxicology · 2023Article
- The Crystal Structure of Mouse Ces2c, a Potential Ortholog of Human CES2, Shows Structural Similarities in Substrate Regulation and Product Release to Human CES1.International journal of molecular sciences · 2022Article
- Pathophysiology and Biomarker Potential of Fatty Acid Ethyl Ester Elevation During Alcoholic Pancreatitis.Gastroenterology · 2021Article
- Human carboxylesterases and fluorescent probes to image their activity in live cells.RSC medicinal chemistry · 2021Review
- Nuclear-lipid-droplet proteome: carboxylesterase as a nuclear lipase involved in lipid-droplet homeostasis.Heliyon · 2021Article
- Polyisoprenylated Cysteinyl Amide Inhibitors: A Novel Approach to Controlling Cancers with Hyperactive Growth Signaling.Current medicinal chemistry · 2021Article
- Detection of carboxylesterase by a novel hydrosoluble near-infrared fluorescence probe.RSC advances · 2019Article
- Overcoming insecticide resistance through computational inhibitor design.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Combined Ensemble Docking and Machine Learning in Identification of Therapeutic Agents with Potential Inhibitory Effect on Human CES1.Molecules (Basel, Switzerland) · 2019Article
- Pharmacometabolomics Informs About Pharmacokinetic Profile of Methylphenidate.CPT: pharmacometrics & systems pharmacology · 2018Article
- Esterase from a cariogenic bacterium hydrolyzes dental resins.Acta biomaterialia · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Human carboxylesterase 1 (hCE1) is a drug and endobiotic-processing serine hydrolase that exhibits relatively broad substrate specificity. It has been implicated in a variety of endogenous cholesterol metabolism pathways including the following apparently disparate reactions: cholesterol ester hydrolysis (CEH), fatty acyl Coenzyme A hydrolysis (FACoAH), acyl-Coenzyme A:cholesterol acyltransfer (ACAT), and fatty acyl ethyl ester synthesis (FAEES). The structural basis for the ability of hCE1 to perform these catalytic actions involving large substrates and products has remained unclear. Here we present four crystal structures of the hCE1 glycoprotein in complexes with the following endogenous substrates or substrate analogues: Coenzyme A, the fatty acid palmitate, and the bile acids cholate and taurocholate. While the active site of hCE1 was known to be promiscuous and capable of interacting with a variety of chemically distinct ligands, these structures reveal that the enzyme contains two additional ligand-binding sites and that each site also exhibits relatively non-specific ligand-binding properties. Using this multisite promiscuity, hCE1 appears structurally capable of assembling several catalytic events depending, apparently, on the physiological state of the cellular environment. These results expand our understanding of enzyme promiscuity and indicate that, in the case of hCE1, multiple non-specific sites are employed to perform distinct catalytic actions.
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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.