Literature summary 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.

Metals/Ions

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

Organism

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

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.14.11.17	dialysis against 25 mM Tris buffer at pH 8.0	Escherichia coli

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	2-aminoethanesulfonic acid/alpha-ketoglutarate dioxygenase	-	Escherichia coli
1.14.11.17	TauD	-	Escherichia coli
1.14.11.17	taurine/alpha-ketoglutarate dioxygenase	-	Escherichia coli

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Release 2023.1 (January 2023)