Molecular Cloning of N-methylputrescine Oxidase from Tobacco | Zendy

Akira Katoh | Zendy; Tsubasa Shoji | Zendy; Takashi Hashimoto | Zendy

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Molecular Cloning of N-methylputrescine Oxidase from Tobacco

Author(s) -

Akira Katoh,

Tsubasa Shoji,

Takashi Hashimoto

Publication year - 2007

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pcm018

Subject(s) - diamine oxidase , nicotiana tabacum , biochemistry , biosynthesis , nicotiana , gene , escherichia coli , mutant , chemistry , cloning (programming) , amine oxidase (copper containing) , biology , enzyme , solanaceae , computer science , programming language

Nicotine biosynthesis in Nicotiana species requires an oxidative deamination of N-methylputrescine, catalyzed by N-methylputrescine oxidase (MPO). In a screen for tobacco genes that were down-regulated in a tobacco mutant with altered regulation of nicotine biosynthesis, we identified two homologous MPO cDNAs which encode diamine oxidases of a particular subclass. Tobacco MPO genes were expressed specifically in the root, and up-regulated by jasmonate treatment. Recombinant MPO protein expressed in Escherichia coli formed a homodimer and deaminated N-methylputrescine more efficiently than symmetrical diamines. These results indicate that MPO evolved from general diamine oxidases to function effectively in nicotine biosynthesis.

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