Double site saturation mutagenesis of the human cytochrome P450 2D6 results in regioselective steroid hydroxylation
Article first published online: 3 MAY 2013
© 2013 The Authors Journal compilation © 2013 FEBS
Special Issue: Catalytic Mechanisms by Biological Systems
Volume 280, Issue 13, pages 3094–3108, July 2013
How to Cite
Geier, M., Braun, A., Fladischer, P., Stepniak, P., Rudroff, F., Hametner, C., Mihovilovic, M. D. and Glieder, A. (2013), Double site saturation mutagenesis of the human cytochrome P450 2D6 results in regioselective steroid hydroxylation. FEBS Journal, 280: 3094–3108. doi: 10.1111/febs.12270
- Issue published online: 18 JUN 2013
- Article first published online: 3 MAY 2013
- Accepted manuscript online: 30 MAR 2013 06:42AM EST
- Manuscript Accepted: 27 MAR 2013
- Manuscript Revised: 26 MAR 2013
- Manuscript Received: 1 FEB 2013
- OXYGREEN. Grant Number: 212281
- DK Molecular Enzymology. Grant Number: FWF W901-B12
- TU-Innovative project METASPECS
Fig. S1. 1H NMR spectrum of the metabolite formed by CYP2D6_E216F_F483G. The assignments of the resonances to 2,17-dihydroxy-, (2β,17β)-androst-4-en-3-one are indicated.
Doc. S1. Modification of synthetic CYP2D6 variants.
Table S1. Relative testosterone hydroxylase activities of all 400 CYP2D6 mutants generated in this study.
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