Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 93:216-221 (1990)
© 1990 American Society of Plant Biologists

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Metabolism and Enzymology

Diamine Oxidase from Cultured Roots of Hyoscyamus niger

Its Function in Tropane Alkaloid Biosynthesis

Takashi Hashimoto, Akira Mitani and Yasuyuki Yamada

Research Center for Cell and Tissue Culture, Faculty of Agriculture, Kyoto University, Kyoto 606, Japan

Diamine oxidase was partially purified from cultured roots of Hyoscyamus niger L. that produce considerable amounts of tropane alkaloids, and then characterized. N-Methylated amines inhibited the activity of the enzyme more strongly than the corresponding primary amines. N-Methylputrescine was the best substrate of those studied, the respective Km values for it and for putrescine and cadaverine being 0.33, 2.85, and 6.25 millimolar. The specificity constants Vmax/Km for putrescine and cadaverine were 11 and 1% of the constant for N-methylputrescine. Marked specificity for the N-methylated diamine would enable the Hyoscyamus enzyme to function specifically in tropane alkaloid biosynthesis.





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