EC number:2.1.1.44
| ID: | 2.1.1.44 |
|---|---|
| Description: | L-histidine N(alpha)-methyltransferase. |
| Alternative Name: |
Dimethylhistidine N-methyltransferase. |
| Cath: | 3.40.50.150; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.44 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.44 |
| KEGG Enzyme Link: | KEGG2.1.1.44 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.44 |
| ExPASy Enzyme Link: | ExPASy2.1.1.44 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.44 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.44 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.44 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.44 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.44 |
| RHEA:38471 | L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine + 3 S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6].[*:7]-[S+;H0:8](-[*:9])-[CH3;+0:10].[*:11]-[S+;H0:12](-[*:13])-[CH3;+0:14]>>[*:1]-[N+;H0:2](-[CH3;+0:10])(-[CH3;+0:14])-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5].[*:7]-[S;H0;+0:8]-[*:9].[*:11]-[S;H0;+0:12]-[*:13] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The enzymatic alpha-N-methylation of histidine. | Ishikawa Y, Melville DB | 1970 Nov 25 | 5484456 |
| Ergothioneine biosynthetic methyltransferase EgtD reveals the structural basis of aromatic amino acid betaine biosynthesis. | Vit A, Misson L, Blankenfeldt W, Seebeck FP | 2015 Jan 2 | 25404173 |
| In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. | Seebeck FP | 2010 May 19 | 20420449 |