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Literature summary for 1.14.11.17 extracted from

  • Ye, S.; Price, J.C.; Barr, E.W.; Green, M.T.; Bollinger, J.M.; Krebs, C.; Neese, F.
    Cryoreduction of the NO-adduct of taurine:alpha-ketoglutarate dioxygenase (TauD) yields an elusive {FeNO}(8) species (2010), J. Am. Chem. Soc., 132, 4739-4751.
    View publication on PubMed
Search for more literature for 1.14.11.17

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic mechanism, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ binding structure and role in the kinetic mechanism, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
taurine + 2-oxoglutarate + O2 Escherichia coli
-
 sulfite + aminoacetaldehyde + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
taurine + 2-oxoglutarate + O2
-
 Escherichia coli sulfite + aminoacetaldehyde + succinate + CO2
-
 ?
taurine + 2-oxoglutarate + O2 reaction mechanism via two accumulating, kinetically competent intermediates upon reaction of the TauD:Fe(II):RKG:taurine complex with O2 Escherichia coli sulfite + aminoacetaldehyde + succinate + CO2
-
 ?

Subunits

Subunits Comment Organism
additional information Geometric Structure of TauD-{FeNO}7, overview Escherichia coli

Synonyms

Synonyms Comment Organism
TauD
-
 Escherichia coli
TauD-{FeNO}7
-
 Escherichia coli
taurine:alpha-ketoglutarate dioxygenase
-
 Escherichia coli