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Acireductone synthase

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Acireductone synthase
Identifiers
EC no.3.1.3.77
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

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

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  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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