Human steroid and oxysterol 7α-hydroxylase CYP7B1: substrate specificity, azole binding and misfolding of clinically relevant mutants
Version of Record online: 20 FEB 2014
© 2014 FEBS
The FEBS Journal
Volume 281, Issue 6, pages 1700–1713, March 2014
How to Cite
Yantsevich, A. V., Dichenko, Y. V., MacKenzie, F., Mukha, D. V., Baranovsky, A. V., Gilep, A. A., Usanov, S. A. and Strushkevich, N. V. (2014), Human steroid and oxysterol 7α-hydroxylase CYP7B1: substrate specificity, azole binding and misfolding of clinically relevant mutants. The FEBS Journal, 281: 1700–1713. doi: 10.1111/febs.12733
- Issue online: 18 MAR 2014
- Version of Record online: 20 FEB 2014
- Accepted manuscript online: 3 FEB 2014 05:37AM EST
- Manuscript Accepted: 28 JAN 2014
- Manuscript Revised: 23 DEC 2013
- Manuscript Received: 5 AUG 2013
- Canadian Institutes for Health Research
- Novartis Research Foundation
- Swedish Agency for Innovation Systems
- Swedish Foundation for Strategic Research
- Welcome Trust
- Canadian Foundation for Innovation
- Genome Canada through the Ontario Genomics Institute
- Karolinska Institutet
- Knut and Alice Wallenberg Foundation
- Ontario Innovation Trust
- Ontario Ministry for Research and Innovation
- Merck and Co. Inc.
Fig. S1. A carbon monoxide difference spectrum of reduced CYP7B1.
Fig. S2. SDS/PAGE of CYP7B1 mutant forms.
Fig. S3. The HPLC chromatogram of a 25-hydroxycholesterol conversion by CYP7B1. The eluted fractions were further analyzed by LC-MS (inset).
Fig. S4. The HPLC chromatogram of a 5α-androstane-3-β-ol-17-one conversion by CYP7B1. The eluted fractions were further analyzed by LC-MS (inset).
Fig. S5. The multiple sequence alignment of CYP7A1 and CYP7B1 proteins from different organisms.
Fig. S6. NMR analysis of the major product of 25-hydroxycholesterol oxidation by CYP7B1.
Table S1. 1H NMR data for 25-hydroxycholesterol and the product of its conversion by CYP7B1 in CDCl3 (500 MHz).
Table S2. Steroids that showed low or no binding to CYP7B1.
Table S3. Azoles that showed low or no binding to CYP7B1.
Table S4. CYP7B1 mutations, their effects and structural role.
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