Conversion of squalene to the pentacarbocyclic hopene.

Chemistry & biology (2004-04-29)
Dirk J Reinert, Gianni Balliano, Georg E Schulz

The membrane protein squalene-hopene cyclase was cocrystallized with 2-azasqualene and analyzed by X-ray diffraction to 2.13 A resolution. The conformation of this close analog was clearly established, and it agreed with the common textbook presentation. The bound squalene undergoes only small conformational changes during the formation of rings A through D, thus requiring no intermediate. However, ring E formation is hindered by an entropic barrier, which may explain its absence in the steroids. The structure analysis revealed a mobile region between the active center cavity and the membrane, which may melt, opening a passage for squalene and hopene.

Product Number
Product Description

Hop-22(29)-ene solution, 0.1 mg/mL in isooctane, analytical standard