Partial Purification and Properties of S-Adenosylmethionine: (R), (S)-Norlaudanosoline-6-O-Methyltransferase from Argemone platyceras Cell Cultures.

@article{Rueffer1983PartialPA,
  title={Partial Purification and Properties of S-Adenosylmethionine: (R), (S)-Norlaudanosoline-6-O-Methyltransferase from Argemone platyceras Cell Cultures.},
  author={M. Rueffer and N. Nagakura and M. Zenk},
  journal={Planta medica},
  year={1983},
  volume={49 11},
  pages={
          131-7
        }
}
A new enzyme, S-adenosylmethionine: (R), (S)-norlaudanosoline-6-O-methyltransferase, was isolated from the soluble protein extract of A. PLATYCERAS cell cultures and purified approximately 80-fold. This enzyme catalyses the formation of 6-O-methylnorlaudanosoline, and, to a minor extent, 7-O-methylnorlaudanosoline from SAM and (S), as well as (R), norlaudanosoline. The apparent molcular weight of the enzyme is 47000 Dalton. The pH-optimum of the enzyme is 7.5, the temperature optimum, 35… Expand
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