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heteroyohimbine/catharanthus roseus
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Partial purification and characterization of a NADPH dependent tetrahydroalstonine synthase from Catharanthus roseus cell suspension cultures.
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A new enzyme was discovered which specifically hydrogenates the iminium form of cathenamine at position 21 to yield the heteroyohimbine alkaloid tetrahydroalstonine. The enzyme was partially purified (35-fold) from Catharanthus roseus cell suspension cultures. It was shown to use exclusively NADPH
Structural investigation of heteroyohimbine alkaloid synthesis reveals active site elements that control stereoselectivity.
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Plants produce an enormous array of biologically active metabolites, often with stereochemical variations on the same molecular scaffold. These changes in stereochemistry dramatically impact biological activity. Notably, the stereoisomers of the heteroyohimbine alkaloids show diverse pharmacological
Geissoschizine synthase controls flux in the formation of monoterpenoid indole alkaloids in a Catharanthus roseus mutant.
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UNASSIGNED
A Catharanthus roseus mutant accumulates high levels of ajmalicine at the expense of catharanthine and vindoline. The altered chemistry depends on increased expression and biochemical activities of strictosidine β-glucosidase and ajmalicine synthase activities and reduced expression and
Unlocking the diversity of alkaloids in Catharanthus roseus: nuclear localization suggests metabolic channeling in secondary metabolism.
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The extraordinary chemical diversity of the plant-derived monoterpene indole alkaloids, which include vinblastine, quinine, and strychnine, originates from a single biosynthetic intermediate, strictosidine aglycone. Here we report for the first time the cloning of a biosynthetic gene and
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