ID: | 2.1.1.87 |
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Description: | Pyridine 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 2.1.1.87 |
BRENDA Enzyme Link: | BRENDA 2.1.1.87 |
KEGG Enzyme Link: | KEGG2.1.1.87 |
BioCyc Enzyme Link: | BioCyc 2.1.1.87 |
ExPASy Enzyme Link: | ExPASy2.1.1.87 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.87 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.87 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.87 |
IntEnz Enzyme Link: | IntEnz 2.1.1.87 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.87 |
RHEA:16893 | pyridine + S-adenosyl-L-methionine = N-methylpyridinium + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[n;H0;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[n+;H0:6](:[*:7])-[CH3;+0:4] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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N-methylation and quaternization of pyridine in vitro by rabbit lung, liver and kidney N-methyltransferases: an S-adenosyl-L-methionine-dependent reaction. | Damani LA, Shaker MS, Crooks PA, Godin CS, Nwosu C | 1986 Jul | 3751119 |