Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae

Satoshi Yamashita, Hisashi Hemmi, Yosuke Ikeda, Toru Nakayama, Tokuzo Nishino

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)


Although isopentenyl diphosphate-dimethylallyl diphosphate isomerase is thought to be essential for archaea because they use the mevalonate pathway, its corresponding activity has not been detected in any archaea. A novel type of the enzyme, which has no sequence similarity to the known, well-studied type of enzymes, was recently reported in some bacterial strains. In this study, we describe the cloning of a gene of a homologue of the novel bacterial isomerase from a thermoacidophilic archaeon Sulfolobus shibatae. The gene was heterologously expressed in Escherichia coli, and the recombinant enzyme was purified and characterized. The thermostable archaeal enzyme is tetrameric, and requires NAD(P)H and Mg2+ for activity, similar to its bacterial homologues. Using its apoenzyme, we were able to confirm that the archaeal enzyme is strictly dependent on FMN. Moreover, we provide evidence to show that the enzyme also has NADH dehydrogenase activity although it catalyzes the isomerase reaction without consuming any detectable amount of NADH.

Original languageEnglish
Pages (from-to)1087-1093
Number of pages7
JournalEuropean Journal of Biochemistry
Issue number6
Publication statusPublished - 2004 Mar 1


  • Archaea
  • Flavoprotein
  • Isopentenyl diphosphate-dimethylallyl diphosphate isomerase
  • Isoprenoid
  • NADH dehydrogenase

ASJC Scopus subject areas

  • Biochemistry


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