Catalytic mechanism of type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase: Verification of a redox role of the flavin cofactor in a reaction with no net redox change

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

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

Type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase requires redox co-enzymes, i.e., flavin mononucleotide (FMN) and NAD(P)H, for activity, although it catalyzes a non-redox reaction. Spectrometric studies and enzyme assays under anaerobic conditions indicate that FMN is reduced through the reaction and is sufficient for activity. The sole function of NAD(P)H appears to be the reduction of FMN since it could be replaced by an alternate reducing agent. When the enzyme was reconstructed with a flavin analogue, no activity was detected, suggesting that the isomerase reaction proceeds via a radical transfer mechanism.

Original languageEnglish
Pages (from-to)905-910
Number of pages6
JournalBiochemical and biophysical research communications
Volume322
Issue number3
DOIs
Publication statusPublished - 2004 Sep 24

Keywords

  • Archaea
  • DeazaFMN
  • Flavoenzyme
  • Flavoprotein
  • Isomerase
  • Isopentenyl diphosphate
  • Isopentenyl diphosphate:dimethylallyl diphosphate isomerase
  • Isoprenoid
  • Oxidase
  • Oxidoreductase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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