EC number:2.5.1.4
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.5 Transferring alkyl or aryl groups, other than methyl groups |
| 2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date) |
| ID: | 2.5.1.4 |
|---|---|
| Description: | Adenosylmethionine cyclotransferase. |
3D structure
Click one PDB to see exact 3D structure provided by NGL.
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 2.5.1.4 |
| BRENDA Enzyme Link: | BRENDA 2.5.1.4 |
| KEGG Enzyme Link: | KEGG2.5.1.4 |
| BioCyc Enzyme Link: | BioCyc 2.5.1.4 |
| ExPASy Enzyme Link: | ExPASy2.5.1.4 |
| EC2PDB Enzyme Link: | EC2PDB 2.5.1.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.5.1.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.5.1.4 |
| IntEnz Enzyme Link: | IntEnz 2.5.1.4 |
| MEDLINE Enzyme Link: | MEDLINE 2.5.1.4 |
| RHEA:21932 | S-adenosyl-L-methionine = homoserine lactone + S-methyl-5'-thioadenosine |
| RULE(radius=1) | ([*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH2;+0:6]-[*:7])>>[*:1]-[O;H0;+0:2]-[CH2;+0:6]-[*:7].[*: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 |
|---|---|---|---|
| The mechanism of the enzymatic cleavage of S-adenosylmethionine to alpha-amino-gamma-butyrolactone. | MUDD SH | 1959 Jul | 13672964 |
| Enzymatic cleavage of S-adenosylmethionine. | MUDD SH | 1959 Jan | 13610898 |