Abstract
An enzyme has been found in different species of isoquinoline alkaloid-producing plant cell cultures which specifically N-methylates certain (S)-tetrahydroprotoberberine alkaloids such as (S)-canadine and (S)-stylopine at the expense of S-adenosyl-l-methionine (SAM). It was partially purified (90-fold from Eschscholtzia californica cell suspension cultures and characterized. The enzyme has a pH optimum of 8.9, a temperature optimum at 40° and a Mr of about 78 000 ± 10%. The Km for (S)-canadine was determined to be 6.4,μM, for (S)-stylopine 3.1 μM and for SAM 12,μM. The enzyme is inhibited by S-adenosyl-l-homocysteine (SAH with a Ki of 24 μM.
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