1982 Volume 92 Issue 6 Pages 1731-1740
Enzymatic formation of nerolidol was demonstrated by incubation of [14C] farnesyl pyrophosphate with the ultracentrifugal supernatant of cell-free extract of Rhodotorula glutinis. Farnesol was also formed concomitantly with the formation of nerolidol and the ratios of formation of both alcohols were from 1:3 to 1:4. Divalent cation was necessary for the reaction and Mn2+ was much more active than Mg2+ for nerolidol formation. No nerolidol was formed when farnesyl monophosphate or farnesol was used instead of farnesyl pyrophosphate as a substrate. Nerolidyl pyrophosphate or nerolidyl monophosphate could not be detected as an intermediate in the reaction. Based on these observations, nerolidol was presumed to be formed not via nerolidyl pyrophosphate or nerolidyl monophosphate but via a carbonium ion intermediate which was formed by cleavage of the carbon-oxygen bond of farnesyl pyrophosphate. This reaction seems to proceed in a similar manner to the acid hydrolysis of farnesyl pyrophosphate to form nerolidol and farnesol.