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| Content Provider | Springer Nature Link |
|---|---|
| Author | Yoneyama, Naho Morimoto, Hanayo Ye, Chuang Xing Ashihara, Hiroshi Mizu, Kouichi Kato, Misako |
| Copyright Year | 2005 |
| 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. |
| Starting Page | 125 |
| Ending Page | 135 |
| Page Count | 11 |
| File Format | |
| ISSN | 16174615 |
| Journal | Molecular and General Genetics MGG |
| Volume Number | 275 |
| Issue Number | 2 |
| e-ISSN | 16174623 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2005-12-07 |
| Publisher Place | Berlin/Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Caffeine Caffeine synthase Camellia, Theobromine Theobromine synthase Theobroma cacao Animal Genetics and Genomics Plant Genetics & Genomics Microbial Genetics and Genomics Biochemistry Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Medicine Molecular Biology |
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