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Literature summary for 1.14.11.17 extracted from

  • Koehntop, K.D.; Marimanikkuppam, S.; Ryle, M.J.; Hausinger, R.P.; Que, L.
    Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism (2006), J. Biol. Inorg. Chem., 11, 63-72.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II) Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
dialysis against 25 mM Tris buffer at pH 8.0 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
2-aminoethanesulfonic acid/alpha-ketoglutarate dioxygenase
-
Escherichia coli
TauD
-
Escherichia coli
taurine/alpha-ketoglutarate dioxygenase
-
Escherichia coli