Bacterial Expression and HTS Assessment of Soluble Epoxide Hydrolase Phosphatase
| Autor: | Philip Gribbon, Ewgenij Proschak, Franca-Maria Klingler, Sandra K. Wittmann, Markus Wolf |
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| Přispěvatelé: | Publica |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Epoxide hydrolase 2 Phosphatase Biochemistry Gene Expression Regulation Enzymologic Analytical Chemistry law.invention Mice 03 medical and health sciences law Catalytic Domain Escherichia coli Animals Humans Phosphofructokinase 2 Enzyme Inhibitors Epoxide hydrolase Epoxide Hydrolases biology Chemistry Molecular biology Phosphoric Monoester Hydrolases Enzyme assay High-Throughput Screening Assays 030104 developmental biology Solubility Lipid phosphatase activity cardiovascular system Recombinant DNA biology.protein Molecular Medicine Biotechnology |
| Zdroj: | SLAS Discovery. 21:689-694 |
| ISSN: | 2472-5552 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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