دورية أكاديمية
Bacterial Expression and HTS Assessment of Soluble Epoxide Hydrolase Phosphatase.
العنوان: | Bacterial Expression and HTS Assessment of Soluble Epoxide Hydrolase Phosphatase. |
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المؤلفون: | Klingler FM; Institute of Pharmaceutical Chemistry, Goethe University Frankfurt, Frankfurt, Germany., Wolf M; Fraunhofer Institute for Molecular Biology and Environmental Ecology ScreeningPort, Hamburg, Germany., Wittmann S; Institute of Pharmaceutical Chemistry, Goethe University Frankfurt, Frankfurt, Germany., Gribbon P; Fraunhofer Institute for Molecular Biology and Environmental Ecology ScreeningPort, Hamburg, Germany., Proschak E; Institute of Pharmaceutical Chemistry, Goethe University Frankfurt, Frankfurt, Germany proschak@pharmchem.uni-frankfurt.de. |
المصدر: | Journal of biomolecular screening [J Biomol Screen] 2016 Aug; Vol. 21 (7), pp. 689-94. Date of Electronic Publication: 2016 Mar 23. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Sage Publications Country of Publication: United States NLM ID: 9612112 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1552-454X (Electronic) Linking ISSN: 10870571 NLM ISO Abbreviation: J Biomol Screen Subsets: MEDLINE |
أسماء مطبوعة: | Publication: <2004- > : Thousand Oaks, CA : Sage Publications Original Publication: Larchmont, NY : Mary Ann Liebert, Inc., c1996- |
مواضيع طبية MeSH: | Enzyme Inhibitors/*isolation & purification , Epoxide Hydrolases/*antagonists & inhibitors , High-Throughput Screening Assays/*methods , Phosphoric Monoester Hydrolases/*antagonists & inhibitors, Animals ; Catalytic Domain/genetics ; Enzyme Inhibitors/pharmacology ; Escherichia coli/genetics ; Gene Expression Regulation, Enzymologic/genetics ; Humans ; Mice ; Phosphoric Monoester Hydrolases/genetics ; Solubility |
مستخلص: | Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that possesses an epoxide hydrolase and lipid phosphatase activity (sEH-P) at two distinct catalytic domains. While the physiological role of the epoxide hydrolase domain is well understood, the consequences of the phosphatase activity remain unclear. Herein we describe the bacterial expression of the recombinant N-terminal domain of sEH-P and the development of a high-throughput screening protocol using a sensitive and commercially available substrate fluorescein diphosphate. The usability of the assay system was demonstrated and novel inhibitors of sEH-P were identified. (© 2016 Society for Laboratory Automation and Screening.) |
فهرسة مساهمة: | Keywords: enzyme assay; high-throughput screening; phosphatase; soluble epoxide hydrolase |
المشرفين على المادة: | 0 (Enzyme Inhibitors) EC 3.1.3.2 (Phosphoric Monoester Hydrolases) EC 3.3.2.- (Epoxide Hydrolases) EC 3.3.2.10 (EPHX2 protein, human) |
تواريخ الأحداث: | Date Created: 20160325 Date Completed: 20180119 Latest Revision: 20180119 |
رمز التحديث: | 20231215 |
DOI: | 10.1177/1087057116637609 |
PMID: | 27009944 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1552-454X |
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DOI: | 10.1177/1087057116637609 |