A cell-free enzyme of Micrococcus lysodeikticus catalyzed the formation of polyprenyl phosphates ranging in carbon chain from C-20 to C-55 with a predominance of C-40. Homogenates of rabbit liver (or kidney) and yeast catalyzed effectively the hydrolysis of these long chain prenyl phosphates, but did not act on the pyrophosphate esters. It was found that lecithin stimulated markedly the chain-elongation catalyzed by the crude enzyme and that it did not affect the synthesis of polyprenyl pyrophosphates by the purified polyprenyl pyrophosphate synthetase directly. The cis, trans configuration of these products was also discussed.