5hiw

Publication Abstract from PubMed

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 Delta4 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 6beta-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.

Structure-function analysis for the hydroxylation of Delta4 C21-steroids by the myxobacterial CYP260B1.,Salamanca-Pinzon SG, Khatri Y, Carius Y, Keller L, Muller R, Lancaster CR, Bernhardt R FEBS Lett. 2016 Jun;590(12):1838-51. doi: 10.1002/1873-3468.12217. Epub 2016 Jun , 3. PMID:27177597^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.