ExplorEnz: EC 1.13.11.53

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1.13.11.53

Accepted name:

acireductone dioxygenase (Ni²⁺-requiring)

Reaction:

1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O₂ = 3-(methylsulfanyl)propanoate + formate + CO

For diagram of methionine salvage, click here and for diagram of reaction, click here

Glossary:

acireductone = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one

Other name(s):

ARD; 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous); acireductone dioxygenase (ambiguous); E-2; 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming)

Systematic name:

1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming)

Comments:

Requires Ni²⁺. If iron(II) is bound instead of Ni²⁺, the reaction catalysed by EC 1.13.11.54, acireductone dioxygenase [iron(II)-requiring], occurs instead [1]. The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Wray, J.W. and Abeles, R.H. A bacterial enzyme that catalyzes formation of carbon monoxide. J. Biol. Chem. 268 (1993) 21466–21469. [PMID: 8407993]
2.	Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147–3153. [DOI] [PMID: 7852397]
3.	Furfine, E.S. and Abeles, R.H. Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J. Biol. Chem. 263 (1988) 9598–9606. [PMID: 2838472]
4.	Dai, Y., Wensink, P.C. and Abeles, R.H. One protein, two enzymes. J. Biol. Chem. 274 (1999) 1193–1195. [DOI] [PMID: 9880484]
5.	Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. ¹H, ¹³C and ¹⁵N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae. J. Biomol. NMR 14 (1999) 287–288. [PMID: 10481280]
6.	Dai, Y., Pochapsky, T.C. and Abeles, R.H. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry 40 (2001) 6379–6387. [DOI] [PMID: 11371200]
7.	Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry 41 (2002) 6761–6769. [DOI] [PMID: 12022880]
8.	Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9 (2002) 966–972. [DOI] [PMID: 12402029]

[EC 1.13.11.53 created 2006]