| ID: | 2.1.1.94 |
|---|---|
| Description: | Tabersonine 16-O-methyltransferase. |
| Alternative Name: |
methyltransferase. S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline 11-O- 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase. 11-demethyl-17-deacetylvindoline 11-methyltransferase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.1.1.94 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.94 |
| KEGG Enzyme Link: | KEGG2.1.1.94 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.94 |
| ExPASy Enzyme Link: | ExPASy2.1.1.94 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.94 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.94 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.94 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.94 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.94 |
| RHEA:20992 | 16-hydroxytabersonine + S-adenosyl-L-methionine = 16-methoxytabersonine + H(+) + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A pair of tabersonine 16-hydroxylases initiates the synthesis of vindoline in an organ-dependent manner in Catharanthus roseus. | Besseau S, Kellner F, Lanoue A, Thamm AM, Salim V, Schneider B, Geu-Flores F, Höfer R, Guirimand G, Guihur A, Oudin A, Glevarec G, Foureau E, Papon N, Clastre M, Giglioli-Guivarc'h N, St-Pierre B, Werck-Reichhart D, Burlat V, De Luca V, O'Connor SE, Courdavault V | 2013 Dec | 24108213 |
| Application of carborundum abrasion for investigating the leaf epidermis: molecular cloning of Catharanthus roseus 16-hydroxytabersonine-16-O-methyltransferase. | Levac D, Murata J, Kim WS, De Luca V | 2008 Jan | 18053006 |