Stereospecificity of cinnamyl alcohol dehydrogenase and synthesis of stereospecifically labelled coniferyl alcohol

Abstract

Abstract-Using horse liver alcohol dehydrogenase, stereospecifically tritiated (R)-and (S)-(y-3H)-coniferyl alcohol was synthesized.Using both of these substrates it was demonstrated that cinnamyl alcohol dehydrogenase from lignifying Forsythia tissue specifically removes the pro-R-hydrogen atom of coniferyl alcohol in the oxidation to the aldehyde. This also means that in the reverse reaction the A-hydrogen of NADPH is transferred to the Re-site of coniferyl aldehyde.

Phytoalexins: Enzymology and Molecular Biology

“…The enzymes responsible for the formation of coniferyl aldehyde and coniferyl alcohol (cinnamoyl CoA : NADP-reductase and cinnamyl alcohol : NADP-dehydrogenase) have been isolated from a number of plant species (584)(585)(586). The stereochemistry of the formation of coniferyl alcohol from feruloyl CoA has been elucidated (587,588), and a mechanism of action has been proposed for the cinnamyl alcohol : NADP-dehydrogenase from Glycine ~ ( 5 8 8 ) .…”

Synthèse des Aldehydespara-Hydroxycinnamiques Substrats de l'Alcool Cinnamylique Deshydrogénase

“…La methode de synthese retenue utilisant les sels d'iminium parait bien adaptee ä la serie para hydroxycinnamique. En effet la methode enzymatique (Klischies et al 1978), par oxydation de l'alcool cinnamylique conduit ä de faibles quantites d'aldehydes. Quant aux methodes chimiques classiques par reduction d'un chlorure d'acide (Freudenberg et Dillenburg 1951;Nakamura et al 1974) ou bien par reaction des para hydroxybenzaldehydes sur les dihydro-1,3 diazines (Nakamura et Higuchi 1976), elles exigent des etapes de protection de la fonction phenol (sous forme d'acetate ou d'ethers) et de deprotection qui contribuent ä abaisser le rendement des syntheses.…”