PARTIAL PURIFICATION AND PROPERTIES OF S-ADENOSYL-L-METHIONINE: (S)-TETRAHYDROPROTOBERBERINE-CIS-N-METHYLTRANSFERASE FROM SUSPENSION-CULTURED CELLS OF ESCHSCHOLTZIA AND CORYDALIS
An enzym 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 deg C and a Mr of about 78000 +/- 10 percent.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.
Rueffer, Martina,Zumstein, Gitta,Zenk, Meinhart H.
p. 3727 - 3733
(2007/10/02)
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