ChemInform Abstract: Enzymatic Formation of Raucaffricine, the Major Indole Alkaloid of Rauwolfia serpentina Cell-Suspension Cultures.

ChemInform ◽  
2010 ◽  
Vol 23 (10) ◽  
pp. no-no
Author(s):  
C. M. RUYTER ◽  
J. H. H. STOECKIGT
1994 ◽  
Vol 72 (1) ◽  
pp. 51-55 ◽  
Author(s):  
Ralf Lutterbach ◽  
Carl Michael Ruyter ◽  
Joachim Stöckigt

From cell suspension cultures of Rauwolfia serpentina Benth. a new enzyme activity was isolated and its properties determined. The enzyme is a soluble protein and catalyzes the transfer of a glucose moiety from UDPG to a wide variety of phenolic compounds with p-nitrophenol as one of the best substrates (Km = 1.21 mM, UDPG = 0.54 mM). In contrast to the membrane-bound UDPG: vomilenine-21-OH-β-D-glucosyltransferase from Rauwolfia serpentina cells, this enzyme is not able to glucosylate indole alkaloids. The enzyme activity has been detected in 14 callus cultures belonging to 10 different plant families.


1988 ◽  
Vol 43 (7-8) ◽  
pp. 479-484 ◽  
Author(s):  
Carl Michael Ruyter ◽  
Helmut Schübel ◽  
Joachim Stöckigt

From cell suspension cultures of Rauwolfia serpentina grown in an optimized production medium for the glucoalkaloid raucaffricine, a novel glucoalkaloid was isolated and identified as 17-O-acetyl-21-O-β-ᴅ-glucopyranosyl-ajmaline (acetylrauglucine). This alkaloid is formed in very small amounts (< 5 × 10-4%). The biogenetically related Nα-demethylated base (acetyl-nor-rauglucine) and the deacetyl product rauglucine have also been detected in culture extracts. In addition 21(.R)-(β-D-glucopyranosyl)-hydroxy-sarpagan-17-al has been isolated and identified as an artifact which originates from raucaffricine.


Sign in / Sign up

Export Citation Format

Share Document