| adenosylmethionine hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.3.1.2 | ||||||||
| CAS no. | 37288-62-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an adenosylmethionine hydrolase (EC 3.3.1.2) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + H2O L-homoserine + methylthioadenosine
L-homoserine + methylthioadenosineThus, the two substrates of this enzyme are S-adenosyl-L-methionine and H2O, whereas its two products are L-homoserine and methylthioadenosine.
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds involving sulfur (thioether and trialkylsulfonium hydrolases). The systematic name of this enzyme class is S-adenosyl-L-methionine hydrolase. Other names in common use include S-adenosylmethionine cleaving enzyme, methylmethionine-sulfonium-salt hydrolase, and adenosylmethionine lyase.
References
- Mazelis M, Levin B, Mallinson N (1965). "Decomposition of methyl methionine sulfonium salts by a bacterial enzyme". Biochim. Biophys. Acta. 105 (1): 106–14. doi:10.1016/s0926-6593(65)80179-5. PMID 5849106.
| Hydrolases: ether bond (EC 3.3) | |
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| 3.3.1 | |
| 3.3.2 | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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