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Title (Primary) 25-hydroxyvitamin D3 synthesis by enzymatic steroid side-chain hydroxylation with water
Author Warnke, M.; Jung, T.; Dermer, J.; Hipp, K.; Jehmlich, N.; von Bergen, M.; Ferlaino, S.; Fries, A.; Müller, M.; Boll, M.;
Journal Angewandte Chemie-International Edition
Year 2016
Department MOLSYB;
Volume 55
Issue 5
Language englisch;
POF III (all) F11;
UFZ wide themes RU3;
Abstract The hydroxylation of vitamin D3 (VD3, cholecalciferol) side chains to give 25-hydroxyvitamin D3 (25OHVD3) is a crucial reaction in the formation of the circulating and biologically active forms of VD3. It is usually catalyzed by cytochrome P450 monooxygenases that depend on complex electron donor systems. Cell-free extracts and a purified Mo enzyme from a bacterium anaerobically grown with cholesterol were employed for the regioselective, ferricyanide-dependent hydroxylation of VD3 and proVD3 (7-dehydrocholesterol) into the corresponding tertiary alcohols with greater than 99 % yield. Hydroxylation of VD3 strictly depends on a cyclodextrin-assisted isomerization of VD3 into preVD3, the actual enzymatic substrate. This facile and robust method developed for 25OHVD3 synthesis is a novel example for the concept of substrate-engineered catalysis and offers an attractive alternative to chemical or O2 /electron-donor-dependent enzymatic procedures.
ID 17785
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=17785
Warnke, M., Jung, T., Dermer, J., Hipp, K., Jehmlich, N., von Bergen, M., Ferlaino, S., Fries, A., Müller, M., Boll, M. (2016):
25-hydroxyvitamin D3 synthesis by enzymatic steroid side-chain hydroxylation with water
Angew. Chem.-Int. Edit. 55 (5), 1881 - 1884