Structure-function analysis for the hydroxylation of Δ4 C21-steroids by the myxobacterial CYP260B1.
FEBS Lett
; 590(12): 1838-51, 2016 06.
Article
em En
| MEDLINE
| ID: mdl-27177597
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 6ß-OH-RSS. The substrate-free crystal structure of CYP260B1 (PDB 5HIW) 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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Esteroide Hidroxilases
/
Proteínas de Bactérias
/
Myxococcales
/
Cortodoxona
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Alemanha