Solanesyl pyrophosphate synthetase from Micrococcus lysodeikticus.

Solanesyl pyrophosphate synthetase from extracts of Micrococcus lysodeikticus was purified by DEAE-Sephadex, hydroxylapatite, and Sephadex G-100 chromatography. This enzyme was found to catalyze the trans condensation of isopentenyl pyrophosphate with geranyl pyrophosphate to afford all-trans-octaprenyl (C40) and alltrans-nonaprenyl (C45) pyrophosphate without accumulation of prenyl pyrophosphate with chain length shorter than C40. all-trans-Farnesyl and all-trans-geranylgeranyl pyrophosphate also were active as cosubstrates, though they were less effective than geranyl pyrophosphate. However, neither dimethylallyl nor cis,trans,trans-geranylgeranyl pyrophosphate was active. The molecular weight of this enzyme was estimated to be 78 000 by Sephadex G-100 filtration. An enzyme preparation from young shoots of potato was found to hydrolyze the polyprenyl pyrophosphates effectively to give the corresponding prenols.