Adenosylmethionine cyclotransferase
| Adenosylmethionine cyclotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.4.1.42 | ||||||||
| CAS no. | 9030-34-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Adenosylmethionine cyclotransferase (EC 4.4.1.42) is an enzyme that catalyzes the chemical reaction
This enzyme has one substrate, S-adenosyl-L-methionine, which cleaves to give initially L-homoserine lactone and 5'-methylthioadenosine. The lactone is converted to homoserine by spontaneous hydrolysis.[1][2][3]
This enzyme was originally described from the yeast Saccharomyces cerevisiae and categorised as a transferase. Later, it was found in bacteriophages and called a hydrolase.[4] However, the bacteriophage enzyme is in fact a lyase with systematic name S-adenosyl-L-methionine lyase.[5][6]
References
- ↑ Mudd, S. Harvey (1959). "Enzymatic Cleavage of S-Adenosylmethionine". Journal of Biological Chemistry. 234: 87–92. doi:10.1016/S0021-9258(18)70340-2. PMID 13610898.
- ↑ Mudd, S. Harvey (1959). "The Mechanism of the Enzymatic Cleavage of S-Adenosylmethionine to α-Amino-γ-butyrolactone". Journal of Biological Chemistry. 234 (7): 1784–1786. doi:10.1016/S0021-9258(18)69926-0. PMID 13672964.
- ↑ Hausmann, Rudolf (1967). "Synthesis of an S -Adenosylmethionine-cleaving Enzyme in T3-infected Escherichia coli and Its Disturbance by Co-infection with Enzymatically Incompetent Bacteriophage". Journal of Virology. 1 (1): 57–63. doi:10.1128/jvi.1.1.57-63.1967. PMC 375505. PMID 4918233.
- ↑ Studier, F. W.; Movva, N. R. (1976). "SAMase gene of bacteriophage T3 is responsible for overcoming host restriction". Journal of Virology. 19 (1): 136–145. doi:10.1128/JVI.19.1.136-145.1976. PMC 354840. PMID 781304.
- ↑ Guo, Xiaohu; Söderholm, Annika; Kanchugal p, Sandesh; Isaksen, Geir V.; Warsi, Omar; Eckhard, Ulrich; Trigüis, Silvia; Gogoll, Adolf; Jerlström-Hultqvist, Jon; Åqvist, Johan; Andersson, Dan I.; Selmer, Maria (2021). "Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family". eLife. 10 e61818. doi:10.7554/eLife.61818. PMC 7877911. PMID 33567250.
- ↑ Enzyme 4.4.1.42 at KEGG Pathway Database.
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