The Purification of Prenyltransferase and Isopentenyl Pyrophosphate Isomerase of Pumpkin Fruit and Their Some Properties

Abstract

Prenyltransferase (farnesyl pyrophosphate synthetase) [EC 2.5.1.1] and isopentenylpyrophosphate isomerase [EG 5.3.3.2] were obtained and partially purified from pumpkin fruit. The prenyltransferase preparation catalyzed the condensation of isopentenyl pyrophosphate with dime-thylallyl pyrophosphate as well as with geranyl pyrophosphate to yield trans-trans 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.