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{{enzyme
| Name = acireductone dioxygenase (Ni2+-requiring)
| EC_number = 1.13.11.53
| CAS_number = 
| IUBMB_EC_number = 1/13/11/53
| GO_code = 0010308
| image = 
| width = 
| caption = 
}}

'''Acireductone dioxygenase (Ni2+-requiring)''' ({{EC number|1.13.11.53}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O<sub>2</sub> <math>\rightleftharpoons</math> 3-(methylthio)propanoate + formate + CO

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[1,2-dihydroxy-5-(methylthio)pent-1-en-3-one]] and [[oxygen]], whereas its 3 [[product (chemistry)|products]] are [[3-(methylthio)propanoate]], [[formate]], and [[carbon monoxide]].

This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on single donors with O<sub>2</sub> as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O<sub>2</sub>.  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'''.  This enzyme participates in [[methionine metabolism]].

==References==
{{reflist|1}}
* {{cite journal | author = Wray JW, Abeles RH | year = 1993 | title = A bacterial enzyme that catalyzes formation of carbon monoxide | journal = J. Biol. Chem.  | volume = 268 | pages = 21466–9  | pmid = 8407993 | issue = 29 }}
* {{cite journal | author = Wray JW, Abeles RH | year = 1995 | title = The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases | journal = J. Biol. Chem.  | volume = 270 | pages = 3147–53  | pmid = 7852397 | issue = 7 | doi=10.1074/jbc.270.7.3147}}
* {{cite journal | author = Furfine ES, Abeles RH | year = 1988 | title = Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae | journal = J. Biol. Chem.  | volume = 263 | pages = 9598–606  | pmid = 2838472 | issue = 20 }}
* {{cite journal | author = Dai Y, Wensink PC, Abeles RH | year = 1999 | title = One protein, two enzymes | journal = J. Biol. Chem.  | volume = 274 | pages = 1193–1195  | pmid = 9880484 | doi = 10.1074/jbc.274.3.1193 | issue = 3 }}
* {{cite journal | author = Mo H, Dai Y, Pochapsky SS, Pochapsky TC | year = 1999 | title = 1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae | journal = J. Biomol. NMR.  | volume = 14 | pages = 287–288  | pmid = 10481280 | doi = 10.1023/A:1008396624784 | issue = 3 }}
* {{cite journal | author = Dai Y, Pochapsky TC, Abeles RH | year = 2001 | title = Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae | journal = Biochemistry.  | volume = 40 | pages = 6379–6387  | pmid = 11371200 | doi = 10.1021/bi010110y | issue = 21 }}
* {{cite journal | author = Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ | year = 2002 | title = XAS investigation of the structure and function of Ni in acireductone dioxygenase | journal = Biochemistry.  | volume = 41 | pages = 6761–6769  | pmid = 12022880 | doi = 10.1021/bi012209a | issue = 21 }}
* {{cite journal | author = Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ | year = 2002 | title = Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae | journal = Nat. Struct. Biol.  | volume = 9 | pages = 966–972  | pmid = 12402029 | doi = 10.1038/nsb863 | issue = 12 }}

[[Category:EC 1.13.11]]
[[Category:Enzymes of unknown structure]]