Acireductone dioxygenase (Ni2+-requiring)
| acireductone dioxygenase (Ni2+-requiring) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.53 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Acireductone dioxygenase (Ni2+-requiring) (EC 1.13.11.53) is an enzyme that catalyzes the chemical reaction
- 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 3-(methylthio)propanoate + formate + CO
Thus, the two substrates of this enzyme are 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and oxygen, whereas its 3 products are 3-(methylthio)propanoate, formate, and carbon monoxide.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming). Other names in common use include ARD, 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous), acireductone dioxygenase (ambiguous), and E-2. This enzyme participates in methionine metabolism.
References
[edit]- Wray JW, Abeles RH (1993). "A bacterial enzyme that catalyzes formation of carbon monoxide". J. Biol. Chem. 268 (29): 21466–9. doi:10.1016/S0021-9258(20)80559-6. PMID 8407993.
- Wray JW, Abeles RH (1995). "The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases". J. Biol. Chem. 270 (7): 3147–53. doi:10.1074/jbc.270.7.3147. PMID 7852397.
- Furfine ES, Abeles RH (1988). "Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae". J. Biol. Chem. 263 (20): 9598–606. doi:10.1016/S0021-9258(19)81558-2. PMID 2838472.
- Dai Y, Wensink PC, Abeles RH (1999). "One protein, two enzymes". J. Biol. Chem. 274 (3): 1193–1195. doi:10.1074/jbc.274.3.1193. PMID 9880484.
- Mo H, Dai Y, Pochapsky SS, Pochapsky TC (1999). "1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae". J. Biomol. NMR. 14 (3): 287–288. doi:10.1023/A:1008396624784. PMID 10481280.
- Dai Y, Pochapsky TC, Abeles RH (2001). "Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae". Biochemistry. 40 (21): 6379–6387. doi:10.1021/bi010110y. PMID 11371200.
- Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ (2002). "XAS investigation of the structure and function of Ni in acireductone dioxygenase". Biochemistry. 41 (21): 6761–6769. doi:10.1021/bi012209a. PMID 12022880.
- Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ (2002). "Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae". Nat. Struct. Biol. 9 (12): 966–972. doi:10.1038/nsb863. PMID 12402029.
