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Peroxidase Catalyzed Dimerization and Demethylation of Protoberberine Alkaloids *
Author(s) -
Bauer W.,
Stadler R.,
Zenk M. H.
Publication year - 1992
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1992.tb00315.x
Subject(s) - peroxidase , berberidaceae , demethylation , ranunculaceae , papaveraceae , benzylisoquinoline , chemistry , stereochemistry , enzyme , yield (engineering) , alkaloid , biochemistry , biology , botany , biosynthesis , materials science , metallurgy , gene , dna methylation , gene expression
A peroxidase which catalyzes, in essentially quantitative yield, the dimerization of jatrotthizine to 4,4′‐bisjatrorrhizine was isolated and partly characterized from Berberis stolonifera cell cultures. This peroxidase also mediates the demethylation of a variety of 10‐ or 3‐O‐CH 3 substituted tetrahydroprotoberberines and their quarternary analogues. A survey of more than 30 cell culture species, using seven different alkaloids, demonstrated the presence of this catalytic activity mainly in the plant families Berberidaceae and Ranunculaceae, while it was absent in the Papaveraceae. Caution is justified when employing alkaloids labelled at their [‐O‐CH 3 ] groups for enzymatic assays except when peroxidases (even without addition of H 2 O 2 ) are not present.