| adenosylmethionine cyclotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.4 | ||||||||
| CAS no. | 9030-34-6 | ||||||||
| 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 cyclotransferase ( EC 2.5.1.4) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine 5'-methylthioadenosine + 2-aminobutan-4-olide
Hence, this enzyme has one substrate, S-adenosyl-L-methionine, and two products, 5'-methylthioadenosine and 2-aminobutan-4-olide.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine alkyltransferase (cyclizing). This enzyme is also called adenosylmethioninase.
References
- Mudd SH (January 1959). "Enzymatic cleavage of S-adenosylmethionine". The Journal of Biological Chemistry. 234 (1): 87–92. PMID 13610898.
- Mudd SH (July 1959). "The mechanism of the enzymatic cleavage of S-adenosylmethionine to alpha-amino-gamma-butyrolactone". The Journal of Biological Chemistry. 234 (7): 1784–6. PMID 13672964.
