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Acireductone dioxygenase (EC 1.13.11.54) is an enzyme that catalyzes the chemical reaction

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O₂ ${\displaystyle \rightleftharpoons }$ 4-(methylthio)-2-oxobutanoate + formate

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

• 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): 1193–5. 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): 287–8. doi:10.1023/A:1008396624784. PMID 10481280. S2CID 36731035.
• Dai Y, Pochapsky TC, Abeles RH (2001). "Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae". Biochemistry. 40 (21): 6379–87. 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): 6761–9. 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): 966–72. doi:10.1038/nsb863. PMID 12402029. S2CID 38098047.

• Biology

• EC 1.13.11
• Enzymes of known structure