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Literature summary for 1.14.11.17 extracted from

  • John, C.W.; Hausinger, R.P.; Proshlyakov, D.A.
    Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD (2019), J. Am. Chem. Soc., 141, 15318-15326 .
    View publication on PubMed
Search for more literature for 1.14.11.17

Protein Variants

Protein Variants Comment Organism
D101Q the variant suppress the conformational change, supporting the involvement in the structural rearrangement. The initial reduction E1/2 in D101Q TauD decreases by 50 mV relative to the wild-type enzyme, reaching comparable values at the end of the reduction. While the initial exponential phase of the oxidationof D101Q is very similar to that of the wild-type protein, oxidation does not continue beyond 100 s Escherichia coli
H255Q the variant suppress the conformational change, supporting the involvement in the structural rearrangement. Both the reduction and oxidation E1/2 are lower in H255Q TauD than in wild-type enzyme, with no noticeable oxidative reorganization. The reductive reorganization for this protein reaches saturation after 1200 s Escherichia coli
H99A the variant shows a larg net redox change relative to the wild-type protein, suggesting that redox-coupled protonation of H99 is required for high redox potentials of the metal Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme has an exceedingly large redox hysteresis between the stable ferric and ferrous forms of up to 468 mV in the wild-type protein and 497 mV in the D101Q variant 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 the nonheme active site of TauD provides a flexible environment that allows the enzyme to modulate its redox potential reversibly by up to 0.5 V. All three amino acid ligands of the iron center (H99, D101, and H255) are intricately involved in the redox-linked structural rearrangement that also affects the protein backbone Escherichia coli sulfite + aminoacetaldehyde + succinate + CO2
-
 ?
taurine + 2-oxoglutarate + O2
-
 Escherichia coli K12 sulfite + aminoacetaldehyde + succinate + CO2
-
 ?
taurine + 2-oxoglutarate + O2 the nonheme active site of TauD provides a flexible environment that allows the enzyme to modulate its redox potential reversibly by up to 0.5 V. All three amino acid ligands of the iron center (H99, D101, and H255) are intricately involved in the redox-linked structural rearrangement that also affects the protein backbone Escherichia coli K12 sulfite + aminoacetaldehyde + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
TauD
-
 Escherichia coli