35 インド蛇木培養細胞から得られた鎖状モノテルペン1級アルコール脱水素酵素の反応(ポスター発表の部)

DOI

書誌事項

タイトル別名
  • 35 PURIFICATION, PROPERTIES AND STEREOSPECIFICITY OF ACYCLIC MONOTERPENE PRIMARY ALCOHOL : NADP^+ OXIDOREDUCTASE FROM RAUWOLFIA SERPENTINA

抄録

Acyclic monoterpene primary alcohol: NADP^+ oxidoreductase, the key enzyme in the biosynthesis of monoterpene alcohols and iridoids in plants, is unstable and has been only poorly characterized. However we have established the conditions to stabilize the enzyme from Rauwolfia serpentina cells, followed by purification of it to homogeneity. It is a monomer with a molecular weight of about 44,000 and contains zinc ions. Various branched - chain allylic primary alcohols such as nerol (6), geraniol (7) and 10-hydroxygeraniol (1) were good substrates, but ethanol was inert. Menthol (16), cyclic monoterpene secondary alcohol, was also inert as a substrate, but inhibited the enzyme competitively. The enzyme exclusively requires NADP^+ or NADPH as the cofactor. Steady - state kinetic studies showed that the dehydrogenation proceeds by an ordered Bi - Bi mechanism. NADP^+ binds the enzyme first and then NADPH is the second product released from it. Neral, 10-hydroxygeranial (2) and 10-oxogeraniol (3) were enzymatically reduced in the presence of stereospecifically deuterium - labelled NADPH's. Capillary gas chromatography - mass spectrometric analysis of the products showed that the enzyme exclusively transfers the pro-R hydrogen at C-4 of NADPH.

収録刊行物

詳細情報 詳細情報について

  • CRID
    1390282681051459968
  • NII論文ID
    110006678908
  • DOI
    10.24496/tennenyuki.32.0_260
  • ISSN
    24331856
  • 本文言語コード
    ja
  • データソース種別
    • JaLC
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

問題の指摘

ページトップへ