Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme |
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Authors: | Naho Yoneyama Hanayo Morimoto Chuang-Xing Ye Hiroshi Ashihara Kouichi Mizuno Misako Kato |
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Institution: | (1) Graduate School of Humanities and Sciences, Ochanomizu University, Otsuka, Bunkyo-ku,, 112-8610 Tokyo, Japan;(2) School of Life Sciences, Sun Yat-Sen University, 510275 Guangzhou, China;(3) Department of Biology, Fuculty of Science, Ochanomizu University, Bunkyo-ku, 112-8610 Tokyo, Japan;(4) Faculty of Bioresource of Science, Akita Prefectural University, 010-0195 Akita City, Akita, Japan |
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Abstract: | Caffeine (1,3,7-trimethylxanthine) and theobromine (3,7-dimethylxanthine) are the major purine alkaloids in plants. To investigate
the diversity of N-methyltransferases involved in purine alkaloid biosynthesis, we isolated the genes homologous for caffeine synthase from
theobromine-accumulating plants. The predicted amino acid sequences of N-methyltransferases in theobromine-accumulating species in Camellia were more than 80% identical to caffeine synthase in C. sinensis. However, there was a little homology among the N-methyltransferases between Camellia and Theobroma. The recombinant enzymes derived from theobromine-accumulating plants had only 3-N-methyltransferase activity. The accumulation of purine alkaloids was, therefore, dependent on the substrate specificity of
N-methyltransferase determined by one amino acid residue in the central part of the protein. |
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Keywords: | Caffeine Caffeine synthase Camellia Theobromine Theobromine synthase Theobroma cacao |
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