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Structure-function analysis for the hydroxylation of Δ4 C21-steroids by the myxobacterial CYP260B1.
- Source :
-
FEBS Letters . Jun2016, Vol. 590 Issue 12, p1838-1851. 14p. - Publication Year :
- 2016
-
Abstract
- Myxobacterial CYP260B1 from Sorangium cellulosum was heterologously expressed in Escherichia coli and purified. The in vitro conversion of a small focused substrate library comprised of Δ4 C21-steroids and steroidal drugs using surrogate bovine redox partners shows that CYP260B1 is a novel steroid hydroxylase. CYP260B1 performs the regio- and stereoselective hydroxylation of the glucocorticoid cortodoxone (RSS) to produce 6β-OH-RSS. The substrate-free crystal structure of CYP260B1 (PDB ) was resolved. Docking of the tested ligands into the crystal structure suggested that the C17 hydroxy moiety and the presence of either a keto or a hydroxy group at C11 determine the selectivity of hydroxylation. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 590
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 116395420
- Full Text :
- https://doi.org/10.1002/1873-3468.12217