BW A4C and other hydroxamic acids are potent inhibitors of linoleic acid 8R-dioxygenase of the fungus Gaeumannomyces graminis
| Autor: | Mats Hamberg, Irene D. Brodowsky, Ernst H. Oliw |
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| Rok vydání: | 1994 |
| Předmět: |
Stereochemistry
Linoleic acid Benzeneacetamides Buffers Hydroxamic Acids chemistry.chemical_compound Lipoxygenase Dioxygenase medicine Lipoxygenase Inhibitors Isomerases Pharmacology chemistry.chemical_classification Glutathione Peroxidase Hydroxamic acid biology Xylariales Acetohydroxamic acid Glutathione Nordihydroguaiaretic acid Intramolecular Oxidoreductases Enzyme chemistry Enzyme inhibitor biology.protein medicine.drug |
| Zdroj: | European journal of pharmacology. 254(1-2) |
| ISSN: | 0014-2999 |
| Popis: | Linoleic acid is converted to 8 R -hydroperoxylinoleic acid by the soluble 8 R -dioxygenase of the fungus Gaeumannomyces graminis . Effects of different lipoxygenase inhibitors on the 8 R -dioxygenase were evaluated. Three hydroxamic acid derivatives were investigated. BW A4C ( N -(3-phenoxycinnamyl)acetohydroxamic acid) was the most potent with an IC 50 of 0.2 μM, followed by zileuton (3–10 μM) and linoleate-hydroxamic acid (0.02 mM). Two other lipoxygenase inhibitors, nordihydroguaiaretic acid and eicosatetraynoic acid, were less potent (IC 50 0.09 and 0.15 mM, respectively). The 8 R -dioxygenase was also strongly inhibited by commonly used buffer additives, dithiothreitol, β-mercaptoethanol and phenylmethanesulfonyl fluoride. G. graminis also contains a hydroperoxide isomerase, which converts 8 R -hyroperoxylinoleic acid to 7S,8 S -dihydroxylinoleic acid. Ammonium sulphate precipitation and gel filtration indicated that the dioxygenase and the hydroperoxide isomerase activities could be seperated. |
| Databáze: | OpenAIRE |
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