Helvetica Chimica Acta · 1991 · 16 citations · 11 references
Life SciencesPlant BiologyPlant SciencesEnzymologyPlant BiochemistryPlant Molecular BiologyAlkaloid BiosynthesisEnzyme KineticsPlant EnzymesPlant MetabolismPlant Natural Product BiosynthesisAlkaloid GlycosylationAlkaloid MetabolismEnzymatic Pathways In Alkaloid BiosynthesisIndole ChemistryPlant GlycoalkaloidsSubstrate Specificity DeterminantsTerpenoid-indole Alkaloid BiosynthesisTransferase Catalysis
Abstract The major alkaloid from Rauwolfia serpentina cell‐suspension cultures, the glucoalkaloid raucaffricine ( 2 ), was enzymatically formed from vomilenine ( 1 ) and UDPG in presence of microsomal‐bound enzyme. This glucosyltransferase exhibits a relatively high substrate specificity with strong preference for 1 and UDPG. The apparent K m values for 1 and UDPG were 40 μ M and 0.8 m M , respectively, for raucaffricine formation. Optimum transferase activity was observed at 50° and pH 6.3. The taxonomic distribution of this enzyme seems to be very limited because transferase can he exclusively detected in raucaffricine‐producing plant cells.
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