EC number:3.13.1.8
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.13 Acting on carbon-sulfur bonds |
| 3.13.1 Acting on carbon-sulfur bonds (only sub-subclass identified to date) |
| ID: | 3.13.1.8 |
|---|---|
| Description: | S-adenosyl-L-methionine hydrolase (adenosine-forming). |
| Alternative Name: |
SAM hydroxide adenosyltransferase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.13.1.8 |
| BRENDA Enzyme Link: | BRENDA 3.13.1.8 |
| KEGG Enzyme Link: | KEGG3.13.1.8 |
| BioCyc Enzyme Link: | BioCyc 3.13.1.8 |
| ExPASy Enzyme Link: | ExPASy3.13.1.8 |
| EC2PDB Enzyme Link: | EC2PDB 3.13.1.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.13.1.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.13.1.8 |
| IntEnz Enzyme Link: | IntEnz 3.13.1.8 |
| MEDLINE Enzyme Link: | MEDLINE 3.13.1.8 |
| RHEA:56140 | H2O + S-adenosyl-L-methionine = adenosine + H(+) + L-methionine |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[S+;H0:3](-[*:4])-[*:5].[OH2;+0:6]>>[*:1]-[CH2;+0:2]-[OH;+0:6].[*:4]-[S;H0;+0:3]-[*:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62). | Deng H, McMahon SA, Eustáquio AS, Moore BS, Naismith JH, O'Hagan D | 2009 Oct 12 | 19739191 |
| S-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved bacterial and archaeal protein related to SAM-dependent halogenases. | Eustáquio AS, Härle J, Noel JP, Moore BS | 2008 Sep 22 | 18720493 |