Abstract

Abstract Soluble enzyme preparations from leaves of Foeniculum vulgare catalysed the pyridine nucleotide-dependent dehydrogenation of l-endo -fenchol to d -fenchone, while similar preparations from Tanacetum vulgare catalysed the pyridine nucleotide-dependent dehydrogenation of d -3-thujanol to d -3-thujone. The monoterpenol dehydrogenases were separated from alcohol (ethanol) dehydrogenase by gel-permeation chromatography, and the MW, pH optimum, cofactor preference and other general properties of these enzymes were examined. Specificity studies indicated that only a narrow range of monoterpenols, related to those structural classes produced in vivo , were oxidized by these dehydrogenases.

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