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Literature summary for 1.14.11.17 extracted from

  • Li, M.; Henderson, K.L.; Martinez, S.; Hausinger, R.P.; Emerson, J.P.
    The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD) (2018), J. Biol. Inorg. Chem., 23, 785-793.
    View publication on PubMed
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Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ isothermal titration calorimetry and related biophysical techniques are used to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to the 2-His-1-carboxylate facial triad of TauD Escherichia coli
Fe2+ nonheme Fe2+-dependent metalloenzyme. The metal-dependent active site in TauD is formed by two histidine and an aspartate side-chains coordinating to one face of the octahedral coordination geometry (2-His-1-carboxylate facial triad) Escherichia coli
Mn2+ isothermal titration calorimetry and related biophysical techniques are used to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to the 2-His-1-carboxylate facial triad of TauD Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P37610
-
-
Escherichia coli K12 P37610
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
TauD
-
 Escherichia coli
taurine/alpha-ketoglutarate dioxygenase
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme catalyzes the hydroxylation of taurine eventually leading to sulfite production in Escherichia coli Escherichia coli