Isolated from the plants Valeriana officinalis (valerian) and Persicaria hydropiper (water pepper). The enzyme does not act on farnesol or drimenol diphosphate. Using 18-oxygen labelled water 18-oxygen was incorporated suggesting involvement of a stabilised carbocation or an equivalent species.
The enzyme appears in viruses and cellular organisms
Isolated from the plants Valeriana officinalis (valerian) and Persicaria hydropiper (water pepper). The enzyme does not act on farnesol or drimenol diphosphate. Using 18-oxygen labelled water 18-oxygen was incorporated suggesting involvement of a stabilised carbocation or an equivalent species.
Substrates: possible intermediates, farnesol and drimenyl diphosphate, cannot be converted to drimenol, suggesting that the intermediate remains tightly bound during catalysis. Enzyme likely uses protonation-initiated cyclization Products: -
expression in yeast and plants results in production of drimenol alone. Coexpression of PhDS with DOX1 in yeast yields drimendiol, the 12-hydroxylation product of drimenol, as a major product, and cinnamolide. By transient expression of drimenol synthase and DOX1 in Nicotiana benthamiana leaves, drimenol is almost completely converted into cinnamolide and several additional drimenol derivatives
mutation of the first Asp residue of the DDxxD motif, known to ionize the substrate in concert with Mg2+. Mutant is unable to ionize substrate farnesyl diphosphate
Partial purification of farnesyl pyrophosphate:drimenol cyclase and geranylgeranyl pyrophosphate:sclareol cyclase, using cell culture as a source of material
Henquet, M.G.L.; Prota, N.; van der Hooft, J.J.J.; Varbanova-Herde, M.; Hulzink, R.J.M.; de Vos, M.; Prins, M.; de Both, M.T.J.; Franssen, M.C.R.; Bouwmeester, H.; Jongsma, M.
Identification of a drimenol synthase and drimenol oxidase from Persicaria hydropiper, involved in the biosynthesis of insect deterrent drimanes
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