Biology:Acireductone synthase
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Short description: Class of enzymes
| Acireductone synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.3.77 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Acireductone synthase (EC number 3.1.3.77, E1, E-1 enolase-phosphatase) is an enzyme with systematic name 5-(methylsulfanyl)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing).[1][2][3] It catalyses the following reaction:
- 5-(methylsulfanyl)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate (overall reaction)
- (1a) 5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate (probably spontaneous)
- (1b) 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
References
- ↑ "Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae". The Journal of Biological Chemistry 268 (33): 24785–91. November 1993. PMID 8227039.
- ↑ "The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases". The Journal of Biological Chemistry 270 (7): 3147–53. February 1995. doi:10.1074/jbc.270.7.3147. PMID 7852397.
- ↑ "Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity". Journal of Molecular Biology 348 (4): 917–26. May 2005. doi:10.1016/j.jmb.2005.01.072. PMID 15843022.
External links
- Acireductone+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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