EC number:2.1.1.60
| ID: | 2.1.1.60 |
|---|---|
| Description: | Calmodulin-lysine N-methyltransferase. |
| Cath: | 3.40.50.150; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.60 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.60 |
| KEGG Enzyme Link: | KEGG2.1.1.60 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.60 |
| ExPASy Enzyme Link: | ExPASy2.1.1.60 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.60 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.60 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.60 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.60 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.60 |
| RHEA:21556 | [calmodulin]-L-lysine + S-adenosyl-L-methionine = [calmodulin]-N(6)-methyl-L-lysine + H(+) + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[NH;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Calmodulin N-methyltransferase. Partial purification and characterization. | Rowe PM, Wright LS, Siegel FL | 1986 May 25 | 3700427 |
| Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin. | Magnani R, Dirk LM, Trievel RC, Houtz RL | 2010 Jul 27 | 20975703 |