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Literature summary for 1.14.11.17 extracted from

  • John, C.W.; Swain, G.M.; Hausinger, R.P.; Proshlyakov, D.A.
    Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD (2019), J. Phys. Chem. B, 123, 7785-7793.
    View publication on PubMed
Search for more literature for 1.14.11.17

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ fully reversible redox-linked conformational changes in three forms of TauD. The hysteresis between the oxidation and reduction Nernstian NPSV profiles arises primarily from isomerization between two separate ferric/ferrous redox couples of the protein 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
-
 ?
taurine + 2-oxoglutarate + O2 Escherichia coli K12
-
 sulfite + aminoacetaldehyde + succinate + CO2
-
 ?

Organism

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

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
-
 Escherichia coli K12 sulfite + aminoacetaldehyde + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
TauD
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme metabolizes taurine as a sulfur source for sulfur-starved cells. TauD activates taurine via hydrogen atom transfer to an Fe(IV)=O intermediate Escherichia coli