ID: | 2.1.1.111 |
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Description: | Anthranilate N-methyltransferase. |
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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: | |
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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 |
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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 |