Species: Hyoscyamus niger
Subunit composition of N-methylputrescine oxidase = [diamine oxidase]2
Molecular Weight of Polypeptide: 66 kD (experimental) [Hashimoto90 ]
Molecular Weight of Multimer: 135 kD (experimental) [Hashimoto90]
Enzymatic reaction of: N-methylputrescine oxidase
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
An N-methylputrescine oxidase has been partially purified from Hyoscyamus niger. The enzyme accepts N-methylputrescine, putrescine, and cadaverine as substrates, with N-methylputrescine being the best substrate. Inhibition of the enzyme activity by copper ligands and carbonyl reagents indicated that copper and pyrroloquinoline quinine are present at the active site of the enzyme.
Inhibitors (Unknown Mechanism): Cu2+ [Hashimoto90] , Hg2+ [Hashimoto90] , p-chloromercuribenzenesulfonic acid [Hashimoto90] , CdCl2 [Hashimoto90] , potassium cyanide [Hashimoto90] , N-methylpropylamine [Hashimoto90] , N-methylbutylamine [Hashimoto90]
pH(opt): 7.5-8 [Hashimoto90]
Hashimoto90: Hashimoto T, Mitani A, Yamada Y (1990). "Diamine Oxidase from Cultured Roots of Hyoscyamus niger: Its Function in Tropane Alkaloid Biosynthesis." Plant Physiol 93(1);216-221. PMID: 16667438
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