Acireductone dioxygenase (iron(II)-requiring)

Class of enzymes From Wikipedia, the free encyclopedia

Acireductone dioxygenase [iron(II)-requiring] (EC 1.13.11.54) is an enzyme that catalyzes the chemical reaction

2D representation of the chemical structure of Q27121564.
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one
 
O2
 
Rightward reaction arrow with minor substrate(s) from top left
 
 
 
2D representation of the chemical structure of Q27093278.
4-(methylthio)-2-oxobutanoic acid
+
 

The two substrates of this enzyme are 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and oxygen. Its products are 4-(methylthio)-2-oxobutanoic acid and formic acid.[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-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. 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 (Ni2+-requiring), which uses nickel(II) rather than iron(II) as the metal at the centre of the active site.[7][8][9]

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2HJI.

References

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