Biology:Acireductone dioxygenase (iron(II)-requiring)
| acireductone dioxygenase [iron(II)-requiring] | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.13.11.54 | ||||||||
| 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 [iron(II)-requiring] (EC 1.13.11.54) is an enzyme that catalyzes the chemical reaction
- 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 4-(methylthio)-2-oxobutanoate + formate
Thus, the two substrates of this enzyme are 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and oxygen, whereas its two products are 4-methylthio-2-oxobutanoate and formate.
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-forming). Other names in common use include ARD', 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous), acireductone dioxygenase (ambiguous), E-2', and E-3 dioxygenase. This enzyme participates in methionine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2HJI.
References
- "A bacterial enzyme that catalyzes formation of carbon monoxide". J. Biol. Chem. 268 (29): 21466–9. 1993. PMID 8407993.
- "The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases". J. Biol. Chem. 270 (7): 3147–53. 1995. doi:10.1074/jbc.270.7.3147. PMID 7852397.
- "Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae". J. Biol. Chem. 263 (20): 9598–606. 1988. PMID 2838472.
- "One protein, two enzymes". J. Biol. Chem. 274 (3): 1193–5. 1999. doi:10.1074/jbc.274.3.1193. PMID 9880484.
- "1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae". J. Biomol. NMR 14 (3): 287–8. 1999. doi:10.1023/A:1008396624784. PMID 10481280.
- "Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae". Biochemistry 40 (21): 6379–87. 2001. doi:10.1021/bi010110y. PMID 11371200.
- "XAS investigation of the structure and function of Ni in acireductone dioxygenase". Biochemistry 41 (21): 6761–9. 2002. doi:10.1021/bi012209a. PMID 12022880.
- "Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae". Nat. Struct. Biol. 9 (12): 966–72. 2002. doi:10.1038/nsb863. PMID 12402029.
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