| ID: | 2.1.1.250 |
|---|---|
| Description: | [Trimethylamine--corrinoid protein] Co-methyltransferase. |
| Alternative Name: |
Trimethylamine 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 2.1.1.250 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.250 |
| KEGG Enzyme Link: | KEGG2.1.1.250 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.250 |
| ExPASy Enzyme Link: | ExPASy2.1.1.250 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.250 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.250 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.250 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.250 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.250 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:39287 | [Co(I) trimethylamine-specific corrinoid protein] + H(+) + trimethylamine = [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine |
| RULE(radius=1) | [*:1]-[N;H0;+0:2](-[*:3])-[CH3;+0:4].[Co+;H0:5].[H+;H0:6]>>[*:1]-[NH;+0:2]-[*:3].[CH3;+0:4]-[Co+2;H0:5] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. | Ferguson DJ Jr, Krzycki JA | 1997 Feb | 9006042 |
| Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. | Krzycki JA | 2004 Oct | 15450490 |