Acireductone dioxygenase (iron(II)-requiring) explained

acireductone dioxygenase [iron(II)-requiring]
Ec Number:	1.13.11.54
Go Code:	0010309

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 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 .

References

• Wray JW, Abeles RH . 1993 . A bacterial enzyme that catalyzes formation of carbon monoxide . J. Biol. Chem. . 268 . 21466 - 9 . 8407993 . 29 . 10.1016/S0021-9258(20)80559-6 . free .
• 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 . 3147 - 53 . 7852397 . 7 . 10.1074/jbc.270.7.3147. free .
• Furfine ES, Abeles RH . 1988 . Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae . J. Biol. Chem. . 263 . 9598 - 606 . 2838472 . 20 . 10.1016/S0021-9258(19)81558-2 . free .
• Dai Y, Wensink PC, Abeles RH . 1999 . One protein, two enzymes . J. Biol. Chem. . 274 . 1193 - 5 . 9880484 . 10.1074/jbc.274.3.1193 . 3 . free.
• 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 . 287 - 8 . 10481280 . 10.1023/A:1008396624784 . 3 . 36731035 .
• Dai Y, Pochapsky TC, Abeles RH . 2001 . Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae . Biochemistry . 40 . 6379 - 87 . 11371200 . 10.1021/bi010110y . 21 .
• Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ . 2002 . XAS investigation of the structure and function of Ni in acireductone dioxygenase . Biochemistry . 41 . 6761 - 9 . 12022880 . 10.1021/bi012209a . 21 .
• 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 . 966 - 72 . 12402029 . 10.1038/nsb863 . 12 . 38098047 .