Acireductone synthase
| Acireductone synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.77 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| 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). It catalyses the following overall reaction:
The enzyme characterised from Klebsiella pneumoniae and rat liver hydrolyses 5-(methylsulfanyl)-2,3-dioxopentyl phosphate to 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and orthophosphate (Pi). This is part of the methionine salvage pathway.[1][2] The crystal structure of the enzyme showed that the mechanism involves an enol of the starting diketone.[3]
References
- ↑ Myers RW, Wray JW, Fish S, Abeles RH (November 1993). "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. doi:10.1016/S0021-9258(19)74533-5. PMID 8227039.
- ↑ Wray JW, Abeles RH (February 1995). "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. doi:10.1074/jbc.270.7.3147. PMID 7852397.
- ↑ Wang H, Pang H, Bartlam M, Rao Z (May 2005). "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. doi:10.1016/j.jmb.2005.01.072. PMID 15843022.
External links
- Acireductone+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Category:
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