@Article{IPB-2263,
author = {Irmler, S. and Schröder, G. and St-Pierre, B. and Crouch, N. P. and Hotze, M. and Schmidt, J. and Strack, D. and Matern, U. and Schröder, J.},
title = {{Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450 CYP72A1 as secologanin synthase}},
year = {2000},
pages = {797-804},
journal = {Plant J.},
doi = {10.1111/j.1365-313X.2000.00922.x},
volume = {24},
abstract = {The molecular characterization of CYP72A1 from Catharanthus roseus  (Madagascar periwinkle) was described nearly a decade ago, but the enzyme function remained unknown. We now show by in situ  hybridization and immunohistochemistry that the expression in immature leaves is epidermis‐specific. It thus follows the pattern previously established for early enzymes in the pathway to indole alkaloids, suggesting that CYP72A1 may be involved in their biosynthesis. The early reactions in that pathway, i.e. from geraniol to strictosidine, contain several candidates for P450 activities. We investigated in this work two reactions, the conversion of 7‐deoxyloganin to loganin (deoxyloganin 7‐hydroxylase, DL7H) and the oxidative ring cleavage converting loganin into secologanin (secologanin synthase, SLS). The action of DL7H has not been demonstrated in vitro  previously, and SLS has only recently been identified as P450 activity in one other plant. We show for the first time that both enzyme activities are present in microsomes from C . roseus  cell cultures. We then tested whether CYP72A1 expressed in E. coli  as a translational fusion with the C . roseus  P450 reductase (P450Red) has one or both of these activities. The results show that CYP72A1 converts loganin into secologanin.}    
}