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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
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

In enzymology, an O-acetylhomoserine aminocarboxypropyltransferase (EC 2.5.1.49) is an enzyme that catalyzes the chemical reaction

O-acetyl-L-homoserine + methanethiol

\rightleftharpoons

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. Vol. 17B. pp. 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. doi:10.1093/oxfordjournals.jbchem.a131339. 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. doi:10.1093/oxfordjournals.jbchem.a130505. 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.