Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus

Hisashi Hemmi, Satoru Ikejiri, Satoshi Yamashita, Tokuzo Nishino

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


Two open reading frames which encode the homologues of (all-E) prenyl diphosphate synthase are found in the whole-genome sequence of Sulfolobus solfataricus, a thermoacidophilic archaeon. It has been suggested that one is a geranylgeranyl diphosphate synthase gene, but the specificity and biological significance of the enzyme encoded by the other have remained unclear. Thus, we isolated the latter by the PCR method, expressed the enzyme in Escherichia coli cells, purified it, and characterized it. The archaeal enzyme, 281 amino acids long, is highly thermostable and requires Mg2+ and Triton X-100 for full activity. It catalyzes consecutive E-type condensations of isopentenyl diphosphate with an allylic substrate such as geranylgeranyl diphosphate and yields the medium-chain product hexaprenyl diphosphate. Despite such product specificity, phylogenetic analysis revealed that the archaeal medium-chain prenyl diphosphate synthase is distantly related to the other medium- and long-chain enzymes but is closely related to eucaryal short-chain enzymes.

Original languageEnglish
Pages (from-to)615-620
Number of pages6
JournalJournal of bacteriology
Issue number3
Publication statusPublished - 2002
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology


Dive into the research topics of 'Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus'. Together they form a unique fingerprint.

Cite this