A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities
نویسندگان
چکیده
منابع مشابه
Mechanism of the Generation of New Somatic Compatibility Groups within Thanatephorus cucumeris (Rhizoctonia solani)
Single-basidiospore isolates (SBIs) were obtained from field isolates of Thanatephorus cucumeris (Rhizoctonia solani) AG-1 IC and AG-2-2 IV. Formation of distinctive tufts, a recognized feature of heterokaryon synthesis, was observed, and isolates derived from hyphal-tipped tuft hyphae were obtained following pairings between various strains. Three distinctive types of tufts were formed: the fi...
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The steroid 20-hydroxyecdysone (20E) is the primary regulatory hormone that mediates developmental transitions in insects and other arthropods. 20E is produced from ecdysone (E) by the action of a P450 monooxygenase that hydroxylates E at carbon 20. The gene coding for this key enzyme of ecdysteroidogenesis has not been identified definitively in any insect. We show here that the Drosophila E-2...
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Central Laboratories for Key Technologies, Kirin Co., Kanazawa-ku, Yokohama, Kanagawa 236-0004, Japan (N.U.); RIKEN Center for Sustainable Resource Science, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan (N.U., K.O., K.S.); Graduate School of Agricultural Science, Kobe University, Nada-ku, Kobe, Hyogo 657-8501, Japan (M.N., M.M.); Department of Chemistry and Materials Science, Tokyo Institute o...
متن کاملTwo Cytochrome P450 Monooxygenases Catalyze Early Hydroxylation Steps in the Potato Steroid Glycoalkaloid Biosynthetic Pathway.
α-Solanine and α-chaconine, steroidal glycoalkaloids (SGAs) found in potato (Solanum tuberosum), are among the best-known secondary metabolites in food crops. At low concentrations in potato tubers, SGAs are distasteful; however, at high concentrations, SGAs are harmful to humans and animals. Here, we show that POTATO GLYCOALKALOID BIOSYNTHESIS1 (PGA1) and PGA2, two genes that encode cytochrome...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2018
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.00503-18