Acireductone synthase

Acireductone synthase (EC 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 + H2O 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate (overall reaction)
(1a) 5-(methylthio)-2,3-dioxopentyl phosphate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate (probably spontaneous)
(1b) 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate + H2O 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate
Acireductone synthase
Identifiers
EC number3.1.3.77
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

References

  1. 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. PMID 8227039.
  2. 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.
  3. 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.
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