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Literature summary for 1.13.11.53 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 1.13.11.53

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis Klebsiella oxytoca

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ dependent on 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 3-(methylthio)propanoate + formate + CO
-
 ?
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 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
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