Abstract
An enzyme (cinchoninone :NADPH oxidoreductase) which catalyses the reduction of cinchoninone to an unequal mixture of cinchonine and cinchonidine has been isolated from cells of Cinchona ledgeriana in suspension culture and its properties have been studied. It is present in two isoenzymic forms which can be separated by ionexchange chromatography on DEAE-cellulose. Both forms of the enzyme are cytosolic and have an absolute requirement for NADPH. They both catalyse reversible reactions. Isoenzyme I acts specifically on cinchoninone in the forward direction and cinchonidine, cinchonine, cupreine and cupreidine in the reverse direction, while isoenzyme II has a broad specificity acting on all the quinoline alkaloids of Cinchona. The kinetic properties of these two isoenzymes are presented. This is the first description of an enzyme wholly committed to the biosynthesis of Cinchona quinoline alkaloids.
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