1.14.11.17: taurine dioxygenase
This is an abbreviated version!
For detailed information about taurine dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.17
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1.14.11.17
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non-heme
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alphakg-dependent
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aminoacetaldehyde
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desulfonation
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self-hydroxylation
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feiv-oxo
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alkanesulfonate
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quintet
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oxygenolytic
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analysis
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biotechnology
- 1.14.11.17
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non-heme
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alphakg-dependent
- aminoacetaldehyde
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desulfonation
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self-hydroxylation
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feiv-oxo
-
alkanesulfonate
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quintet
-
oxygenolytic
- analysis
- biotechnology
Reaction
Synonyms
2-aminoethanesulfonate dioxygenase, 2-aminoethanesulfonic acid/alpha-ketoglutarate dioxygenase, alpha-ketoglutarate-dependent dioxygenase, alpha-ketoglutarate-dependent taurine dioxygenase, alpha-ketoglutarate/taurine dioxygenase, AtsK, Fe(II)/2-oxoglutarate-dependent taurine dioxygenase, Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase, oxygenative alkylsulfatase, SSI3, TauD, TauD-{FeNO}7, taurine (2-aminoethanesulfonate)/2-oxoglutarate dioxygenase, taurine alpha ketoglutarate dioxygenase, taurine alpha-ketoglutarate dioxygenase, taurine dioxygenase, taurine hydroxylase, taurine-alpha-ketoglutarate dioxygenase, taurine/2-oxoglutarate dioxygenase, taurine/alpha-ketoglutarate dioxygenase, taurine/alpha-ketoglutarate-dependent dioxygenase, taurine/alphaKG dioxygenase, taurine/alphaKGD, taurine: alpha-ketoglutarate dioxygenase, taurine:2OG dioxygenase, taurine:alpha-ketoglutarate dioxygenase
ECTree
1.14.11.17 taurine dioxygenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.14.11.17 - taurine dioxygenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3-dioxo-2-isoindolineethanesulfonic acid + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
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-
-
-
?
2-oxoglutarate + 2-methylaminoethane-1-sulfonic acid + O2
methylaminoacetaldehyde + succinate + sulfite + CO2
assay at pH 6.2, 30°C
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-
?
4-aminobutyric acid + 2-oxoglutarate + O2
D-2-hydroxy-4-aminobutyric acid + succinate + CO2
activity with mutant enzyme F206Y is 4.7fold higher than activity with wild-type enzyme
-
-
?
5-aminovaleric acid + 2-oxoglutarate + O2
D-2-hydroxy-5-aminovaleric acid + succinate + CO2
activity with mutant enzyme F206Y is 4.4fold higher than activity with wild-type enzyme
-
-
?
6-aminocaproic acid + 2-oxoglutarate + O2
D-2-hydroxy-6-aminocaproic acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
alpha-methyl-beta-alanine + 2-oxoglutarate + O2
3-amino-2-hydroxy-2-methylpropanoic acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
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-
?
beta-alanine + 2-oxoglutarate + O2
D-isoserine + succinate + CO2
activity with mutant enzyme F206Y is 2.4fold higher than activity with wild-type enzyme
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-
?
butanesulfonic acid + 2-oxoglutarate + O2
sulfite + butanal + succinate + CO2
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-
-
-
?
butyric acid + 2-oxoglutarate + O2
2-hydroxybutyric acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
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-
?
hexanesulfonic acid + 2-oxoglutarate + O2
sulfite + hexanal + succinate + CO2
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-
-
-
?
N-methyltaurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + methylaminoacetaldehyde
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-
-
-
?
pentanesulfonic acid + 2-oxoglutarate + O2
sulfite + pentanal + succinate + CO2
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-
-
-
?
propionic acid + 2-oxoglutarate + O2
2-hydroxypropionic acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
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-
?
taurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + aminoacetaldehyde
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-
-
-
?
taurine + 2-oxoglutarate + O2
succinate + CO2 + 2-aminoethanal + sulfite
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-
-
-
?
taurine + alpha-ketoadipate + O2
sulfite + aminoacetaldehyde + pentan-1,5-dioic acid + CO2
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alpha-ketoadipate is less active than 2-oxoglutarate, no activity with pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketocaproate, alpha-ketoisovalerate and oxalacetat
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-
?
valeric acid + 2-oxoglutarate + O2
2-hydroxyvaleric acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
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-
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
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-
-
-
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
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-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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no substrates are methanesulfonic acid, ethanesulfonic acid, isethionic acid, 2-bromoethanesulfonic acid, L-cysteic acid, sulfosuccinate, 4-aminobenzenesulfonic acid, 2-(4-pyridyl)ethanesulfonic acid, N-phenyltaurine
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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enables the use of taurine as sulfur source
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
enables the use of taurine as sulfur source
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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enables the use of taurine as sulfur source
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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reaction mechanism via two accumulating, kinetically competent intermediates upon reaction of the TauD:Fe(II):RKG:taurine complex with O2
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
calculations using large cluster models that include key hydrogen bonding interactions in the substrate binding pocket and His70 protonated reproduce experimental rates and selectivity excellently and give a dominant C1-hydroxylation channel leading to R-1-hydroxytaurine products. This is triggered by charged active site residues including a protonated His70 group
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
calculations using large cluster models that include key hydrogen bonding interactions in the substrate binding pocket and His70 protonated reproduce experimental rates and selectivity excellently and give a dominant C1-hydroxylation channel leading to R-1-hydroxytaurine products. This is triggered by charged active site residues including a protonated His70 group
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-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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-
-
?
additional information
?
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the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
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-
?
additional information
?
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the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
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-
?
