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Partial purification and characterization of dihydrobenzophenanthridine oxidase from Eschscholtzia californica cell suspension cultures

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Abstract

The observation that upon elicitation cell suspension cultures of Eschscholtzia california showed a decrease of dihydromacarpine with a concomittant increase of macarpine led to the discovery of a novel enzyme which catalyzes the oxidation of dihydrobenzophenanthridines in the presence of oxygen. The enzyme was enriched approx. 70-fold. It has a pH-optimum of 7.0, an isoelectric point at pH 8.8, molecular weight of 56 kD and shows a high degree of substrate specificity. The enzyme obviously catalyzes the terminal step in the formation of benzophenanthridine alkaloids containing methylene dioxy substitutions in rings A and D.

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Authors and Affiliations

  1. Lehrstuhl für Pharmazeutische Biologie der Universität München, Karlstrasse 29, D-8000, München 2, Federal Republic of Germany

    H. M. Schumacher & M. H. Zenk

Authors
  1. H. M. Schumacher
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  2. M. H. Zenk
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Communicated by K. Hahlbrock

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Schumacher, H.M., Zenk, M.H. Partial purification and characterization of dihydrobenzophenanthridine oxidase from Eschscholtzia californica cell suspension cultures. Plant Cell Reports 7, 43–46 (1988). https://doi.org/10.1007/BF00272975

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  • DOI: https://doi.org/10.1007/BF00272975

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