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S-Adenosyl-l-methionine: Columbamine-O-methyl transferase, a compartmentalized enzyme in protoberberine biosynthesis

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Abstract

Suspension cultures of Berberis wilsoniae var. subcaulialata and B. aggregata are a useful source for the detection, partial purification and characterization of a new enzyme which specifically transfers the methyl group from (S)-adenosyl-L-methionine to the 2-OH-position of columbamine, thus producing palmatine. The enzyme was enriched approx. 30-fold; it is situated in a vesicle with the density ρ=1.14, has a pH-optimum of 8.9, a molecular weight of 52 kD and shows a high degree of substrate specificity.

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Abbreviations

SAH:

S-adenosyl-L-homocysteine

SAM:

S-Adenosyl-L-methionine

STOX:

(S)-Tetrahydroprotoberberine oxidase

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Authors and Affiliations

  1. Lehrstuhl für Pharmazeutische Biologie der Universität München, Karlstr. 29, D-8000, München 2, Germany

    M. Rueffer, M. Amann & M. H. Zenk

Authors
  1. M. Rueffer
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  2. M. Amann
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  3. M. H. Zenk
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Additional information

Communicated by K. Hahlbrock

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Rueffer, M., Amann, M. & Zenk, M.H. S-Adenosyl-l-methionine: Columbamine-O-methyl transferase, a compartmentalized enzyme in protoberberine biosynthesis. Plant Cell Reports 5, 182–185 (1986). https://doi.org/10.1007/BF00269113

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  • DOI: https://doi.org/10.1007/BF00269113

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