Sesquiterpenes produced by truncated taxadiene synthase

Soluble, highly active N-terminal truncated taxadiene synthase catalyzes the formation of an isomeric mixture of taxadienes from geranylgeranyl diphosphate. Farnesyl diphosphate was also found to be a good substrate, producing four sesquiterpenes which were characterized. The dual activities of taxadiene synthase and product inhibition caused by sesquiterpene metabolites make it imperative that active GGDP synthase be present in order for multi-enzyme systems to follow the taxol pathway in vitro.