EC number:2.1.1.6
| ID: | 2.1.1.6 |
|---|---|
| Description: | Catechol O-methyltransferase. |
| Cath: | 1.10.10.10; 3.40.50.150; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.6 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.6 |
| KEGG Enzyme Link: | KEGG2.1.1.6 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.6 |
| ExPASy Enzyme Link: | ExPASy2.1.1.6 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.6 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.6 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.6 |
| RHEA:17877 | a catechol + S-adenosyl-L-methionine = a guaiacol + 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 |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Multiple molecular forms of catechol-O-methyltransferase. Evidence for two distinct forms, and their purification and physical characterization. | Huh MM, Friedhoff AJ | 1979 Jan 25 | 762061 |
| The purification and properties of pig brain catechol-o-methyltransferase. | Gulliver PA, Tipton KF | 1979 May | 438821 |
| A catechol-O-methyltransferase that is essential for auditory function in mice and humans. | Du X, Schwander M, Moresco EM, Viviani P, Haller C, Hildebrand MS, Pak K, Tarantino L, Roberts A, Richardson H, Koob G, Najmabadi H, Ryan AF, Smith RJ, Müller U, Beutler B | 2008 Sep 23 | 18794526 |
| Comparative study of ortho- and meta-nitrated inhibitors of catechol-O-methyltransferase: interactions with the active site and regioselectivity of O-methylation. | Palma PN, Rodrigues ML, Archer M, Bonifácio MJ, Loureiro AI, Learmonth DA, Carrondo MA, Soares-da-Silva P | 2006 Jul | 16618795 |