Enzyme Characteristics of Amine Oxidase in Lyophyllum aggregatum KUHNEN ("Hon-shimeji")

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Amine oxidase (AO) activity was assayed in 51 species of plants. Among these plants, high AO activity was observed in Lyophyllum aggregatum KUHNEN ("Hon-shimeji") ; some of its properties were investigated. It was found that 96% of the AO activity was localized in the soluble fraction (100000×g sup.). When β-phenylethylamine (PEA) was used as a substrate, the AO activities in mitochondrial (15000×g ppt.) and microsomal fractions (100000×g ppt.) had similar kinetic constants, but that in the soluble fraction was different. Based on inhibition studies, AO in Honshimeji could be classified into two forms. One is a metallo enzyme (containing cupric copper and pyridoxal phosphate) which is inhibited by semicarbazide and cuprizone, and the other is a flavin enzyme which is inhibited by clorgyline.
社団法人日本薬学会の論文
1985-11-25