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Literature summary for 1.14.11.17 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)

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

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

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

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
TauD
-
Escherichia coli
taurine hydroxylase
-
Escherichia coli

General Information

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