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)
書誌事項
- タイトル別名
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- 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
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- 天然有機化合物討論会講演要旨集
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天然有機化合物討論会講演要旨集 32 (0), 260-267, 1990
天然有機化合物討論会実行委員会
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詳細情報 詳細情報について
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- CRID
- 1390282681051459968
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- NII論文ID
- 110006678908
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- ISSN
- 24331856
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可