Partial purification and characterization of geissoschizine dehydrogenase from suspension cultures of Catharanthus roseus |
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| Authors: | Artur Pfitzner Joachim Stöckigt |
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| Affiliation: | Institut für Pharmazeutische Biologie, Universität München, D-8000 München 2, W. Germany |
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| Abstract: | The characterization and partial purification of geissoschizine dehydrogenase from Catharanthus roseus cell suspension cultures are described. The 35-fold purified enzyme removes the 21α-hydrogen of geissoschizine in a NADP+-dependent reaction. NAD+, FAD or FMN cannot act as cofactors for the dehydrogenation. Structurally related indole alkaloids are not dehydrogenated. In comparison to enzymes of the ajmalicine pathway, geissoschizine dehydrogenase shows an extremely low specific activity. |
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| Keywords: | Apocynaceae geissoschizine dehydrogenase stereospecificity biosynthesis heteroyohimbine alkaloids cell suspension culture. |
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