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. 1988 Jan;7(1):43-6.
doi: 10.1007/BF00272975.

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

H M Schumacher  1 , M H Zenk
Affiliations

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

H M Schumacher et al. Plant Cell Rep. 1988 Jan.

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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References

    1. Plant Cell Rep. 1987 Dec;6(6):410-3 - PubMed
    1. Anal Biochem. 1976 May 7;72:248-54 - PubMed