Abstract
Prenyltransferase (farnesyl pyrophosphate synthetase) [EC 2. 5. 1. 1] and isopentenylpyrophosphate isomerase [EC 5. 3. 3. 2] were obtained and partially purified from pumpkin fruit. The prenyltransferase preparation catalyzed the condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate as well as with geranyl pyrophosphate to yield trans-traps farnesyl pyrophosphate as a final product, and was free of isopentenyl pyrophosphate isomerase and geranylgeranyl pyrophosphate synthetase activities. Prenyltransferase of pumpkin has properties similar to those of pig liver, showing requirement of Mg++, Km value of 1.3×10-6M for geranyl pyrophosphate, and pH optimum at 7.5.
