Title |
Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme
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Published in |
Molecular Genetics and Genomics, December 2005
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DOI | 10.1007/s00438-005-0070-z |
Pubmed ID | |
Authors |
Naho Yoneyama, Hanayo Morimoto, Chuang-Xing Ye, Hiroshi Ashihara, Kouichi Mizuno, Misako Kato |
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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Demographic breakdown
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