Solanesyl Pyrophosphate Synthetase from Micrococcus lysodeikticus

Hiroshi Sagami, Kyozo Ogura, Shuichi Seto

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44 Citations (Scopus)


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 all-trans-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-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.

Original languageEnglish
Pages (from-to)4616-4622
Number of pages7
Issue number21
Publication statusPublished - 1977 Oct 1

ASJC Scopus subject areas

  • Biochemistry


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