“O-acetylhomoserine aminocarboxypropyltransferase”的意思、由来-开放百科全书

词条

O-acetylhomoserine aminocarboxypropyltransferase

释义

References

{{enzyme
| Name = O-acetylhomoserine aminocarboxypropyltransferase
| EC_number = 2.5.1.49
| CAS_number = 37290-90-7
| IUBMB_EC_number = 2/5/1/49
| GO_code = 0003961
| image =
| width =
| caption =
}}

In enzymology, an O-acetylhomoserine aminocarboxypropyltransferase ({{EC number|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-methionine 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

{{cite journal | author = Kerr D | date = 1971 | title = O-Acetylhomoserine sulfhydrylase (Neurospora) | journal = Methods Enzymol. | volume = 17B | pages = 446–450 | doi=10.1016/0076-6879(71)17079-6}}
{{cite journal | vauthors = Smith IK, Thompson JF | date = 1969 | title = Utilization of S-methylcysteine and methylmercaptan by methionineless mutants of Neurospora and the pathway of their conversion to methionine. II. Enzyme studies | journal = Biochim. Biophys. Acta | volume = 184 | pages = 130–8 | pmid = 5791104 | issue = 1 | doi=10.1016/0304-4165(69)90107-x}}
{{cite journal | vauthors = Yamagata S, Takeshima K | location = Tokyo | title = O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast Further purification and characterization as a pyridoxal enzyme | journal = J. Biochem. | volume = 80| pages = 777–85 | pmid = 795806 | issue = 4 | date=October 1976 | doi=10.1093/oxfordjournals.jbchem.a131338}}
{{cite journal | author = Yamagata S | location = Tokyo | title = O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast Subunit structure | journal = J. Biochem. | volume = 80| pages = 787–97 | pmid = 795807 | issue = 4 | date=October 1976}}
{{cite journal | vauthors = Yamagata S, Takeshima K, Naiki N | location = Tokyo | title = Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast | journal = J. Biochem. | volume = 75| pages = 1221–9 | pmid = 4609980 | issue = 6 | date=June 1974}}
{{cite journal | author = Yamagata S | date = 1989 | title = Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms | journal = Biochimie | volume = 71 | pages = 1125–43 | pmid = 2517474 | issue = 11–12 | doi=10.1016/0300-9084(89)90016-3}}
{{cite journal | vauthors = Kuramitsu S, Iwama T | date = 2001 | title = Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product | journal = Biochim. Biophys. Acta | volume = 1549 | pages = 61–72 | pmid = 11566369 | issue = 1 | doi = 10.1016/S0167-4838(01)00245-X }}

2 : EC 2.5.1|Enzymes of unknown structure

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