EC number:2.1.1.8
| ID: | 2.1.1.8 |
|---|---|
| Description: | Histamine N-methyltransferase. |
| Cath: | 3.40.50.150; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.8 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.8 |
| KEGG Enzyme Link: | KEGG2.1.1.8 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.8 |
| ExPASy Enzyme Link: | ExPASy2.1.1.8 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.8 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.8 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.8 |
| RHEA:19301 | histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[nH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[n;H0;+0:6](:[*:7])-[CH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The kinetic properties and reaction mechanism of histamine methyltransferase from human skin. | Francis DM, Thompson MF, Greaves MW | 1980 Jun 1 | 7188427 |
| Purification and kinetic properties of ox brain histamine N-methyltransferase. | Gitomer WL, Tipton KF | 1986 Feb 1 | 3707517 |