| ID: | 2.1.1.117 |
|---|---|
| Description: | (S)-scoulerine 9-O-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 2.1.1.117 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.117 |
| KEGG Enzyme Link: | KEGG2.1.1.117 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.117 |
| ExPASy Enzyme Link: | ExPASy2.1.1.117 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.117 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.117 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.117 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.117 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.117 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:23808 | (S)-scoulerine + S-adenosyl-L-methionine = (S)-tetrahydrocolumbamine + 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 |
|---|---|---|---|
| Molecular cloning and characterization of S-adenosyl-L-methionine:scoulerine-9-O-methyltransferase from cultured cells of Coptis japonica. | Takeshita N, Fujiwara H, Mimura H, Fitchen JH, Yamada Y, Sato F | 1995 Jan | 7719631 |
| Characterization of three O-methyltransferases involved in noscapine biosynthesis in opium poppy. | Dang TT, Facchini PJ | 2012 Jun | 22535422 |
| Molecular characterization of O-methyltransferases involved in isoquinoline alkaloid biosynthesis in Coptis japonica. | Morishige T, Tamakoshi M, Takemura T, Sato F | 2010 | 20689233 |