Acireductone synthase

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 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.
  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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.