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Literature summary for 1.13.11.54 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
Search for more literature for 1.13.11.54

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis Klebsiella oxytoca

Metals/Ions

Metals/Ions Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
acireductone dioxygenase
-
 Klebsiella oxytoca
ARD'
-
 Klebsiella oxytoca

General Information

General Information Comment Organism
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
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