EC Number   |
Application |
Reference |
|---|
   2.1.1.53 | analysis |
convenient and accurate enzyme-coupled colorimetric PMT assay, based on the conversion of S-adenosyl-L-homocysteine by 5'-methylthioacenosine/S-adenosylhomocysteine nucleosidase and S-ribosylhomocysteine lyase |
676734 |
| 2.1.1.53 | more |
chimera proteins obtained by fusion of fragments of Solanum tuberosum pmt2 and Hyoscyamus niger pmt are active as PMT |
676699 |
| 2.1.1.53 | more |
different polyamine catabolic processes in hypergeous and hypogeous tissues, duality in polyamine catabolic pathways involves correlation of amine oxidases with PMT for the production of nicotine alkaloids, and with POX for the lignification, cell wall formation, and vascular differentiation |
676574 |
| 2.1.1.53 | more |
no functional protein translated from Solanum tuberosum pmt2, chimera proteins obtained by fusion of fragments of Solanum tuberosum pmt2 and Hyoscyamus niger pmt are active as PMT, if the initial part of pmt2 is used, indicating that a mutation in the terminal part of the gene causes insolubility of the enzyme |
676699 |
| 2.1.1.53 | more |
protein model of PMT based on the crystal structure of SPDS suggests that overall protein folds are comparable, the respective cosubstrates S-adenosylmethionine and decarboxylated S-adenosylmethionine, however, appear to bind differentially to the active sites of both enzymes, and the substrate putrescine adopts a different position |
676557 |
| 2.1.1.53 | more |
the deduced amino acid sequence of Anisodus tanguticus shows 92% identity with both Hyoscyamus niger and Atropa belladonna PMT |
676733 |
| 2.1.1.53 | synthesis |
overexpression of enzyme is not sufficient to boost scopolamine biosynthesis. Simultaneous overexpression of enzyme and hyoscyamine 6 beta-hydroxylase results in sígnificant enhancement of scopolamine accumulation |
663228 |
| 2.1.1.53 | synthesis |
overexpression of enzyme leads to enhanced N-methylputrescine levels, but the subsequent alkaloid metabolites are not affected |
662536 |
