Acireductone dioxygenase (Ni2+-requiring)
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Acireductone dioxygenase (Ni2+-requiring) (EC 1.13.11.53) is an enzyme that catalyzes the chemical reaction
| Acireductone dioxygenase (Ni2+-requiring) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
3D structure of Acireductone dioxygenase | |||||||||
| 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 | ||||||||
| |||||||||
The two substrates of this enzyme are 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and oxygen. Its products are 3-(methylthio)propionic acid, formic acid, and carbon monoxide.[1][2][3][4]
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. It participates in the methionine salvage pathway in the bacterium Klebsiella pneumoniae.[5][6]
The protein component of the enzyme is identical to that in acireductone dioxygenase (iron(II)-requiring), which uses iron(II) rather than nickel(II) as the metal at the centre of the active site.[7][8][9]