O-acetylhomoserine aminocarboxypropyltransferase
| O-acetylhomoserine aminocarboxypropyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.49 | ||||||||
| CAS no. | 37290-90-7 | ||||||||
| 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 O-acetylhomoserine aminocarboxypropyltransferase (EC 2.5.1.49) is an enzyme that catalyzes the chemical reaction
- O-acetyl-L-homoserine + methanethiol L-methionine + acetate
Thus, the two substrates of this enzyme are O-acetyl-L-homoserine and methanethiol, whereas its two products are L-methyionine and acetate.
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 O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase. Other names in common use include O-acetyl-L-homoserine acetate-lyase (adding methanethiol), O-acetyl-L-homoserine sulfhydrolase, O-acetylhomoserine (thiol)-lyase, O-acetylhomoserine sulfhydrolase, and methionine synthase. This enzyme participates in methionine metabolism and cysteine metabolism.
References
- Kerr D (1971). "O-Acetylhomoserine sulfhydrylase (Neurospora)". Methods Enzymol. 17B: 446–450. doi:10.1016/0076-6879(71)17079-6.
- Smith IK, Thompson JF (1969). "Utilization of S-methylcysteine and methylmercaptan by methionineless mutants of Neurospora and the pathway of their conversion to methionine. II. Enzyme studies". Biochim. Biophys. Acta. 184 (1): 130–8. doi:10.1016/0304-4165(69)90107-x. PMID 5791104.
- Yamagata S, Takeshima K (October 1976). "O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast Further purification and characterization as a pyridoxal enzyme". J. Biochem. 80 (4). Tokyo: 777–85. doi:10.1093/oxfordjournals.jbchem.a131338. PMID 795806.
- Yamagata S (October 1976). "O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure". J. Biochem. 80 (4). Tokyo: 787–97. PMID 795807.
- Yamagata S, Takeshima K, Naiki N (June 1974). "Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast". J. Biochem. 75 (6). Tokyo: 1221–9. PMID 4609980.
- Yamagata S (1989). "Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms". Biochimie. 71 (11–12): 1125–43. doi:10.1016/0300-9084(89)90016-3. PMID 2517474.
- Kuramitsu S, Iwama T (2001). "Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product". Biochim. Biophys. Acta. 1549 (1): 61–72. doi:10.1016/S0167-4838(01)00245-X. PMID 11566369.
