Inhibition of Ergosterol Biosynthesis by Morpholine, Piperidine, and Spiroketalamine Fungicides in Microdochium nivale: Effect on Sterol Composition and Sterol Δ8 → Δ7-Isomerase Activity
Autor: | Pierre Leroux, Alain Rahier, Annick Arnold, Christian Malosse, Maryse Taton, Michel Gredt, Danièle Debieu, Jocelyne Bach, Sandrine Brousset |
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Přispěvatelé: | Unité de phytopharmacie et médiateurs chimiques, Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS) |
Rok vydání: | 2000 |
Předmět: |
0106 biological sciences
Isomerase activity Stereochemistry Health Toxicology and Mutagenesis Isomerase Biology FENPROPIMORPH 01 natural sciences MICRODOCHIUM NIVALE 03 medical and health sciences chemistry.chemical_compound Biosynthesis PIPERALIN [SDV.IDA]Life Sciences [q-bio]/Food engineering polycyclic compounds [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering TRIDEMORPH ComputingMilieux_MISCELLANEOUS STEROLS 030304 developmental biology chemistry.chemical_classification 0303 health sciences Fenpropimorph Ergosterol General Medicine Sterol FENPROPIDIN Enzyme FUNGITOXICITY FUNGUS chemistry Tridemorph Biochemistry STEROL DELTA8-DELTA7-ISOMERASE lipids (amino acids peptides and proteins) Agronomy and Crop Science SPIROXAMINE 010606 plant biology & botany |
Zdroj: | Pesticide Biochemistry and Physiology Pesticide Biochemistry and Physiology, Elsevier, 2000, 67 (2), pp.85-94. ⟨10.1006/pest.2000.2485⟩ |
ISSN: | 0048-3575 1095-9939 |
DOI: | 10.1006/pest.2000.2485 |
Popis: | Microdochium nivale , a wheat pathogenic filamentous fungus, appeared to be very sensitive in in vivo laboratory assays to fenpropimorph and tridemorph and to a lesser extent to fenpropidin, piperalin, and spiroxamine. It accumulated Δ 8 -sterols when grown in the presence of one of these sterol biosynthesis inhibitors. Thus, in M. nivale , these fungicides seemed to be very good inhibitors of the sterol Δ 8 → Δ 7 -isomerase. This hypothesis was then confirmed by sterol Δ 8 → Δ 7 -isomerase inhibition assays in cell-free enzyme systems. |
Databáze: | OpenAIRE |
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