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| Name = Acireductone synthase
| EC_number = 3.1.3.77
| CAS_number =
| IUBMB_EC_number = 3/1/3/77
| GO_code =
| image =
| width =
| caption =
}}Acireductone synthase ({{EC number|3.1.3.77}}, E1, E-1 enolase-phosphatase) is an enzyme with systematic name 5-(methylthio)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing).[1][2][3] This enzyme catalyses the following chemical reaction
5-(methylthio)-2,3-dioxopentyl phosphate + H2O1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate (overall reaction)
(1a) 5-(methylthio)-2,3-dioxopentyl phosphate
(1b) 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate + H2O
References
1. ^{{cite journal | vauthors = Myers RW, Wray JW, Fish S, Abeles RH | title = Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae | journal = The Journal of Biological Chemistry | volume = 268 | issue = 33 | pages = 24785–91 | date = November 1993 | pmid = 8227039 }}
2. ^{{cite journal | vauthors = Wray JW, Abeles RH | title = The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases | journal = The Journal of Biological Chemistry | volume = 270 | issue = 7 | pages = 3147–53 | date = February 1995 | pmid = 7852397 | doi = 10.1074/jbc.270.7.3147 }}
3. ^{{cite journal | vauthors = Wang H, Pang H, Bartlam M, Rao Z | title = Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity | journal = Journal of Molecular Biology | volume = 348 | issue = 4 | pages = 917–26 | date = May 2005 | pmid = 15843022 | doi = 10.1016/j.jmb.2005.01.072 }}
2. ^{{cite journal | vauthors = Wray JW, Abeles RH | title = The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases | journal = The Journal of Biological Chemistry | volume = 270 | issue = 7 | pages = 3147–53 | date = February 1995 | pmid = 7852397 | doi = 10.1074/jbc.270.7.3147 }}
3. ^{{cite journal | vauthors = Wang H, Pang H, Bartlam M, Rao Z | title = Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity | journal = Journal of Molecular Biology | volume = 348 | issue = 4 | pages = 917–26 | date = May 2005 | pmid = 15843022 | doi = 10.1016/j.jmb.2005.01.072 }}
External links
- {{MeshName|Acireductone+synthase}}
1 : EC 3.1.3
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