Acireductone dioxygenase (iron(II)-requiring)

In enzymology, an acireductone dioxygenase [iron(II)-requiring] is an enzyme that catalyzes the chemical reaction

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 rightleftharpoons 4-(methylthio)-2-oxobutanoate + formate

Thus, the two substrates of this enzyme are 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one and O2, 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 .


  • Wray JW, Abeles RH "A bacterial enzyme that catalyzes formation of carbon monoxide". J. Biol. Chem. 268 21466–9.
  • Wray JW, Abeles RH "The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases". J. Biol. Chem. 270 3147–53.
  • Furfine ES, Abeles RH "Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae". J. Biol. Chem. 263 9598–606.
  • Dai Y, Wensink PC, Abeles RH "One protein, two enzymes". J. Biol. Chem. 274 1193–5.
  • Mo H, Dai Y, Pochapsky SS, Pochapsky TC "1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae". J. Biomol. NMR. 14 287–8.
  • Dai Y, Pochapsky TC, Abeles RH "Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae". Biochemistry. 40 6379–87.
  • Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ "XAS investigation of the structure and function of Ni in acireductone dioxygenase". Biochemistry. 41 6761–9.
  • Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ "Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae". Nat. Struct. Biol. 9 966–72.

External links

Gene Ontology (GO) codes

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