pARTIAL PURIFICATION AND PROPERTIES OF PRENYLTRANSFERASE FROM PISUM SATIVUM

Article abstract of DOI:10.1016/0031-9422(81)85214-4

Key Wodr Index - Pisum sativum; Leguminosae; pea; prenyltransferase; enzyme purification; farnesyl pyrophosphate. Prenyltransferase (EC 2.5.1.1; assayed as farnesyl pyrophosphate synthetase) was purified 106-fold from an homogenate of 3-day-old seedlings of Pisum sativum.Some of the properties of the purified enzyme were determined and these differed in several significant respect from those reported for preparations from other sources, e.g. the apparent MW was 96000+/-4000 and the preparation could be dissociated into two subunits of MW 45000+/-3000.The total activity of the extractable enzyme went through a sharp maximum (in the range 1 to 28 days) 3 days after germination.Farnesyl pyrophosphate was formed in cell-free extracts of peas from either isopentyl pyrophosphate alone, or this together with geranyl pyrophosphate (optimum yields 1.2 and 10 percent respectively).Use of <1-14C>- and <4-14C>-isopentyl pyrophosphates as the sole substrates and degradation of the products showed that the crude extracts contained a pool of the biogenic equivalent of 3,3-dimethylallyl pyrophosphate.No analogous pool of geranyl pyrophosphate could be detected.