ID: | 2.1.1.250 |
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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: | |
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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 |