Publication Details

Category Text Publication
Reference Category Journals
DOI 10.1002/anie.201510331
Document Shareable Link
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. ORCID logo ; von Bergen, M.; Ferlaino, S.; Fries, A.; Müller, M.; Boll, M.
Source Titel Angewandte Chemie-International Edition
Year 2016
Department MOLSYB
Volume 55
Issue 5
Page From 1881
Page To 1884
Language englisch
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.
Persistent UFZ Identifier
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 10.1002/anie.201510331