| ID: | 2.1.1.12 |
|---|---|
| Description: | Methionine S-methyltransferase. |
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.| UniProtKB Enzyme Link: | UniProtKB 2.1.1.12 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.12 |
| KEGG Enzyme Link: | KEGG2.1.1.12 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.12 |
| ExPASy Enzyme Link: | ExPASy2.1.1.12 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.12 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.12 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.12 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.12 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.12 |
| RHEA:13761 | L-methionine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine |
| RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]-[S;H0;+0:6]-[*:7]>>[*:5]-[S+;H0:6](-[*:7])-[CH3;+0:4].[*:1]-[S;H0;+0:2]-[*:3] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| S-adenosyl-L-methionine:L-methionine S-methyltransferase from germinating barley. Purification and localization. | Pimenta MJ, Kaneta T, Larondelle Y, Dohmae N, Kamiya Y | 1998 Oct | 9765528 |
| Purification and properties of S-adenosyl-L-methionine:L-methionine S-methyltransferase from Wollastonia biflora leaves. | James F, Nolte KD, Hanson AD | 1995 Sep 22 | 7673218 |
| S-methylmethionine plays a major role in phloem sulfur transport and is synthesized by a novel type of methyltransferase. | Bourgis F, Roje S, Nuccio ML, Fisher DB, Tarczynski MC, Li C, Herschbach C, Rennenberg H, Pimenta MJ, Shen TL, Gage DA, Hanson AD | 1999 Aug | 10449582 |