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Literature summary extracted from

  • Allpress, C.J.; Grubel, K.; Szajna-Fuller, E.; Arif, A.M.; Berreau, L.M.
    Regioselective aliphatic carbon-carbon bond cleavage by a model system of relevance to iron-containing acireductone dioxygenase (2013), J. Am. Chem. Soc., 135, 659-668.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.53 crystal structure analysis Klebsiella oxytoca
1.13.11.54 crystal structure analysis Klebsiella oxytoca

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.53 Ni2+ dependent on Klebsiella oxytoca
1.13.11.54 Fe2+ dependent on. Fe2+ transmits electrons from the residues, coordinating it to bound dioxygen and populating its formerly p*-orbital. This leads to dioxygen splitting in the second intermediate and eventual access to the Fe2+-dependent acireductone dioxygenase reaction route Klebsiella oxytoca

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.53 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 Klebsiella oxytoca
-
 4-(methylthio)-2-oxobutanoate + formate
-
 ?
1.13.11.54 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 Klebsiella oxytoca
-
 4-(methylthio)-2-oxobutanoate + formate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.53 Klebsiella oxytoca
-
-
-
1.13.11.54 Klebsiella oxytoca
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.53 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
-
 Klebsiella oxytoca 3-(methylthio)propanoate + formate + CO
-
 ?
1.13.11.53 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
-
 Klebsiella oxytoca 4-(methylthio)-2-oxobutanoate + formate
-
 ?
1.13.11.54 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
-
 Klebsiella oxytoca 4-(methylthio)-2-oxobutanoate + formate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.53 acireductone dioxygenase
-
 Klebsiella oxytoca
1.13.11.53 ARD
-
 Klebsiella oxytoca
1.13.11.54 acireductone dioxygenase
-
 Klebsiella oxytoca
1.13.11.54 ARD'
-
 Klebsiella oxytoca

General Information

EC Number General Information Comment Organism
1.13.11.53 additional information upon splitting of dioxygen, the enzyme immediately decomposes the reacting system into its three experimentally found products. crystal structure analysis, structure modeling and molecular simulations of the Ni2+ and Fe2+ enzyme, cf. 1.13.11.54, QM-DMD domain, overview Klebsiella oxytoca
1.13.11.53 physiological function either facilitates recycling of methionine in living cells or exits this recycling pathway. Ni2+-dependent ARD produces methylthiopropionate, CO, and formate Klebsiella oxytoca
1.13.11.54 additional information Fe2+-dependent acireductone dioxygenase passes through an additional split dioxygen intermediate and then proceeds through an epoxy-like transition state with a small activation energy to the two products, crystal structure analysis, structure modeling and molecular simulations of the Fe2+ and Ni2+ enzyme, cf. 1.13.11.53, QM-DMD domain, overview. The ability of Fe2+-dependent acireductone dioxygenase to stabilize an additional intermediate and thus produce the two products is due to the RedOx flexibility of the Fe2+ as compared to the more electron-rich Ni2+ Klebsiella oxytoca
1.13.11.54 physiological function either facilitates recycling of methionine in living cells or exits this recycling pathway. Fe2+-dependent acireductone dioxygenase produces the 2-oxo acid precursor of methionine and formate Klebsiella oxytoca