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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have