مورد إلكتروني
A peroxygenase from Chaetomium globosum catalyzes the selective oxygenation of testosterone
| العنوان: | A peroxygenase from Chaetomium globosum catalyzes the selective oxygenation of testosterone |
|---|---|
| المصدر: | ChemBioChem : a European journal of chemical biology (2017), 18(6), S. 563-569. ISBN: 1439-7633. DOI: 10.1002/cbic.201600677. |
| بيانات النشر: | Wiley-VCH Verlag 2017-04-03 |
| تفاصيل مُضافة: | Kiebist, Jan Schmidtke, Kai-Uwe Zimmermann, Jörg Kellner, Harald Jehmlich, Nico Ullrich, René Zänder, Daniel Hofrichter, Martin Scheibner, Katrin |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | Unspecific peroxygenases (UPO, EC 1.11.2.1) secreted by fungi open an efficient way to selectively oxyfunctionalize diverse organic substrates, including less-activated hydrocarbons, by transferring peroxide-borne oxygen. We investigated a cell-free approach to incorporate epoxy and hydroxyl functionalities directly into the bulky molecule testosterone by a novel unspecific peroxygenase (UPO) that is produced by the ascomycetous fungus Chaetomium globosum in a complex medium rich in carbon and nitrogen. Purification by fast protein liquid chromatography revealed two enzyme fractions with the same molecular mass (36 kDa) and with specific activity of 4.4 to 12 U mg−1. Although the well-known UPOs of Agrocybe aegerita (AaeUPO) and Marasmius rotula (MroUPO) failed to convert testosterone in a comparative study, the UPO of C. globosum (CglUPO) accepted testosterone as substrate and converted it with total turnover number (TTN) of up to 7000 into two oxygenated products: the 4,5-epoxide of testosterone in β-configuration and 16α-hydroxytestosterone. The reaction performed on a 100 mg scale resulted in the formation of about 90 % of the epoxide and 10 % of the hydroxylation product, both of which could be isolated with purities above 96 %. Thus, CglUPO is a promising biocatalyst for the oxyfunctionalization of bulky steroids and it will be a useful tool for the synthesis of pharmaceutically relevant steroidal molecules. |
| مصطلحات الفهرس: | Peroxidase, Hydroxylierung, Epoxidierung, Steriod, Oxyfunktionalisierung, TU Dresden, Publikationsfonds, peroxidase, hydroxylation, epoxidation, steroid, oxyfunctionalization, TU Dresden, Publishing Fund, info:eu-repo/classification/ddc/540, ddc:540, doc-type:article, info:eu-repo/semantics/article, doc-type:Text |
| URL: | 10.1002/cbic.201600677 |
| الإتاحة: | Open access content. Open access content info:eu-repo/semantics/openAccess |
| ملاحظة: | English |
| أرقام أخرى: | SUUSL oai:qucosa:de:qucosa:30259 urn:nbn:de:bsz:14-qucosa-222847 https://tud.qucosa.de/id/qucosa%3A30259Test https://tud.qucosa.de/api/qucosa%3A30259/attachment/ATT-0Test/ 1135779800 |
| المصدر المساهم: | STAATS U UNIV From OAIster®, provided by the OCLC Cooperative. |
| رقم الانضمام: | edsoai.on1135779800 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |