EC number:2.1.1.292
| ID: | 2.1.1.292 |
|---|---|
| Description: | Carminomycin 4-O-methyltransferase. |
| Cath: | 1.10.10.10; 1.10.287.1350; 3.40.50.150; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.292 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.292 |
| KEGG Enzyme Link: | KEGG2.1.1.292 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.292 |
| ExPASy Enzyme Link: | ExPASy2.1.1.292 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.292 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.292 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.292 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.292 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.292 |
EC number:2.1.1.292
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:38311 | carminomycin + S-adenosyl-L-methionine = daunorubicin + H(+) + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+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 |
|---|---|---|---|
| Partial purification and properties of carminomycin 4-O-methyltransferase from Streptomyces sp. strain C5. | Connors NC, Strohl WR | 1993 Jun | 8360627 |
| Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products. | Jansson A, Koskiniemi H, Mäntsälä P, Niemi J, Schneider G | 2004 Sep 24 | 15273252 |