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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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PMCarticles
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NCBIproteins

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

References

  1. ^ Myers, R.W.; Wray, J.W.; Fish, S.; Abeles, R.H. (1993). "Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae". J. Biol. Chem. 268 (33): 24785–24791. PMID 8227039.
  2. ^ Wray, J.W.; Abeles, R.H. (1995). "The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases". J. Biol. Chem. 270: 3147–3153. doi:10.1074/jbc.270.7.3147. PMID 7852397.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  3. ^ Wang, H.; Pang, H.; Bartlam, M.; Rao, Z. (2005). "Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity". J. Mol. Biol. 348 (4): 917–926. doi:10.1016/j.jmb.2005.01.072. PMID 15843022.