The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
The Purification of Prenyltransferase and Isopentenyl Pyrophosphate Isomerase of Pumpkin Fruit and Their Some Properties
KYOZO OGURA, TOKUZO NISHINO, SHUICHI SETO
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1968 年 64 巻 2 号 p. 197-203

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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.
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© The Japanese Biochemical Society
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