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Literature summary extracted from

  • Casey, T.M.; Grzyska, P.K.; Hausinger, R.P.; McCracken, J.
    Measuring the orientation of taurine in the active site of the non-heme Fe(II)/alpha-ketoglutarate-dependent taurine hydroxylase (TauD) using electron spin echo envelope modulation (ESEEM) spectroscopy (2013), J. Phys. Chem. B, 117, 10384-10394.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.17 enzyme with bound substrate taurine, crystal structure analysis at 2.5 A resolution Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.17 Fe2+ dependent on, non-heme mononuclear Fe(II) center Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.17 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.11.17 taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2 the TauD mechanism begins with the bidentate coordination of 2-oxoglutarate to Fe(II) displacing two water ligands. Taurine then binds to the active site resulting in the displacement of the apical H2O and formation of a 5-coordinate Fe(II) center. O2 binds to the open coordination site on Fe(II), yielding an Fe(III)-superoxo species. Subsequent oxidative decarboxylation of 2-oxoglutarate leads to formation of a Fe(IV)=O intermediate that triggers hydroxylation of the C1 carbon of taurine via hydrogen atom abstraction and radical rebound chemistry The hydroxylated taurine spontaneously decomposes to sulfite and aminoacetaldehyde Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.17 taurine + 2-oxoglutarate + O2
-
 Escherichia coli sulfite + aminoacetaldehyde + succinate + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.17 TauD
-
 Escherichia coli
1.14.11.17 taurine hydroxylase
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
1.14.11.17 additional information structure-activity analysis, modeling and simulations, overview. Modeling of TauD-(Fe-NO) complex and spectral analysis Escherichia coli