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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate (overall reaction)

(1a) 5-(methylthio)-2,3-dioxopentyl phosphate $\rightleftharpoons$ 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate (probably spontaneous)

(1b) 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate + H₂O $\rightleftharpoons$ 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate

References

1. Myers, R.W., Wray, J.W., Fish, S. and 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. and 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. and 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.

External links

• Acireductone synthase at the US National Library of Medicine Medical Subject Headings (MeSH)