| ID: | 2.1.1.111 |
|---|---|
| Description: | Anthranilate N-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 2.1.1.111 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.111 |
| KEGG Enzyme Link: | KEGG2.1.1.111 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.111 |
| ExPASy Enzyme Link: | ExPASy2.1.1.111 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.111 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.111 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.111 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.111 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.111 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:12180 | anthranilate + S-adenosyl-L-methionine = H(+) + N-methylanthranilate + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[NH;+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 |
|---|---|---|---|
| Anthranilate N-methyltransferase, a branch-point enzyme of acridone biosynthesis. | Rohde B, Hans J, Martens S, Baumert A, Hunziker P, Matern U | 2008 Feb | 17988223 |