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Information on EC 1.14.11.17 - taurine dioxygenase
for references in articles please use BRENDA:EC1.14.11.17
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
1.14.11.17 taurine dioxygenase
IUBMB Comments
Requires FeII. The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.14.11.17
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non-heme
-
alphakg-dependent
- aminoacetaldehyde
-
desulfonation
-
self-hydroxylation
-
feiv-oxo
-
alkanesulfonate
-
quintet
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oxygenolytic
- analysis
- biotechnology
showSynonyms
alpha-ketoglutarate-dependent dioxygenase, taurine dioxygenase, taurine/alpha-ketoglutarate dioxygenase, taurine:alpha-ketoglutarate dioxygenase, taurine hydroxylase, alpha-ketoglutarate-dependent taurine dioxygenase, taurine/alphakg dioxygenase, taurine alpha-ketoglutarate dioxygenase, taurine-alpha-ketoglutarate dioxygenase, taurine:2og dioxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-aminoethanesulfonate dioxygenase
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-
-
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alpha-ketoglutarate-dependent dioxygenase
alpha-ketoglutarate-dependent taurine dioxygenase
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-
-
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AtsK
Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase
oxygenative alkylsulfatase
SSI3
-
-
-
-
TauD
taurine/alpha-ketoglutarate dioxygenase
taurine:2OG dioxygenase
TauD
-
-
TauD
-
taurine/alpha-ketoglutarate dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
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-
-
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taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
mechanism
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taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
the TauD mechanism begins with the bidentate coordination of 2-oxoglutarate to Fe(II) displacing two water ligands. Taurine then binds to the active site resulting in the displacement of the apical H2O and formation of a 5-coordinate Fe(II) center. O2 binds to the open coordination site on Fe(II), yielding an Fe(III)-superoxo species. Subsequent oxidative decarboxylation of 2-oxoglutarate leads to formation of a Fe(IV)=O intermediate that triggers hydroxylation of the C1 carbon of taurine via hydrogen atom abstraction and radical rebound chemistry The hydroxylated taurine spontaneously decomposes to sulfite and aminoacetaldehyde
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taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
the key step in the catalytic cycle of the alpha-ketoglutarate-dependent dioxygenases is the hydrogen transfer process. A concerted mechanism takes place, where the H atom transfer happens simultaneously with the electron transfer from taurine to the Fe=O cofactor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
hydroxylation
oxidation
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redox reaction
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reduction
decarboxylation
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the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
hydroxylation
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catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II)
hydroxylation
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the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
reduction
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reduction
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the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
taurine degradation IV
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SYSTEMATIC NAME
IUBMB Comments
taurine, 2-oxoglutarate:O2 oxidoreductase (sulfite-forming)
Requires FeII. The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates.
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CAS REGISTRY NUMBER
COMMENTARY
197809-75-9
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297319-14-3
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325506-70-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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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Substrates: -
Products: -
Products: -
?
2-oxoglutarate + 2-methylaminoethane-1-sulfonic acid + O2
methylaminoacetaldehyde + succinate + sulfite + CO2
Substrates: assay at pH 6.2, 30°C
Products: -
Products: -
?
4-aminobutyric acid + 2-oxoglutarate + O2
D-2-hydroxy-4-aminobutyric acid + succinate + CO2
Substrates: activity with mutant enzyme F206Y is 4.7fold higher than activity with wild-type enzyme
Products: -
Products: -
?
5-aminovaleric acid + 2-oxoglutarate + O2
D-2-hydroxy-5-aminovaleric acid + succinate + CO2
Substrates: activity with mutant enzyme F206Y is 4.4fold higher than activity with wild-type enzyme
Products: -
Products: -
?
6-aminocaproic acid + 2-oxoglutarate + O2
D-2-hydroxy-6-aminocaproic acid + succinate + CO2
Substrates: mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
Products: -
Products: -
?
alpha-methyl-beta-alanine + 2-oxoglutarate + O2
3-amino-2-hydroxy-2-methylpropanoic acid + succinate + CO2
Substrates: mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
Products: -
Products: -
?
beta-alanine + 2-oxoglutarate + O2
D-isoserine + succinate + CO2
Substrates: activity with mutant enzyme F206Y is 2.4fold higher than activity with wild-type enzyme
Products: -
Products: -
?
butanesulfonic acid + 2-oxoglutarate + O2
sulfite + butanal + succinate + CO2
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Substrates: -
Products: -
Products: -
?
butyric acid + 2-oxoglutarate + O2
2-hydroxybutyric acid + succinate + CO2
Substrates: mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
Products: -
Products: -
?
hexanesulfonic acid + 2-oxoglutarate + O2
sulfite + hexanal + succinate + CO2
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Substrates: -
Products: -
Products: -
?
MOPS + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
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Substrates: -
Products: -
Products: -
?
N-methyltaurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + methylaminoacetaldehyde
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Substrates: -
Products: -
Products: -
?
pentanesulfonic acid + 2-oxoglutarate + O2
sulfite + pentanal + succinate + CO2
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Substrates: -
Products: -
Products: -
?
propionic acid + 2-oxoglutarate + O2
2-hydroxypropionic acid + succinate + CO2
Substrates: mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + aminoacetaldehyde
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Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
succinate + CO2 + 2-aminoethanal + sulfite
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Substrates: -
Products: -
Products: -
?
taurine + alpha-ketoadipate + O2
sulfite + aminoacetaldehyde + pentan-1,5-dioic acid + CO2
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Substrates: alpha-ketoadipate is less active than 2-oxoglutarate, no activity with pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketocaproate, alpha-ketoisovalerate and oxalacetat
Products: -
Products: -
?
valeric acid + 2-oxoglutarate + O2
2-hydroxyvaleric acid + succinate + CO2
Substrates: mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
Products: -
Products: -
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
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Substrates: -
Products: -
Products: -
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
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Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: 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
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: enables the use of taurine as sulfur source
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: enables the use of taurine as sulfur source
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: enables the use of taurine as sulfur source
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: reaction mechanism via two accumulating, kinetically competent intermediates upon reaction of the TauD:Fe(II):RKG:taurine complex with O2
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: 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
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: 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
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: 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
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: 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
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
Products: -
Products: -
?
additional information
?
-
-
Substrates: the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: enables the use of taurine as sulfur source
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: enables the use of taurine as sulfur source
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
Substrates: enables the use of taurine as sulfur source
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
isothermal titration calorimetry and related biophysical techniques are used to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to the 2-His-1-carboxylate facial triad of TauD
Cr2+
-
Cr(II) replaces Fe2+ and binds stoichiometrically with 2-oxoglutarate to the Fe(II)/2-oxoglutarate binding site of the protein, with additional Cr(II) used to generate a chromophore attributed to a Cr(III)-semiquinone in a small percentage of the sample. Formation of the semiquinone requires the dihydroxyphenylalanine quinone form of Y73, generated by intracellular self-hydroxylation
Fe
Fe2+
Iron
Mn2+
isothermal titration calorimetry and related biophysical techniques are used to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to the 2-His-1-carboxylate facial triad of TauD
additional information
Fe
-
catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II)
Fe
the enzyme contains a central iron atom that is held in position by interactions with the side chains of two histidine and an aspartic acid residue
Fe2+
-
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview
Fe2+
the thermodynamic properties of Fe2+ binding to the 2-His-1-carboxylate facial triad in alpha-ketoglutarate/taurine dioxygenase (TauD) are explored using isothermal titration calorimetry. Direct titrations of Fe2+ into TauD and chelation experiments involving the titration of thylenediaminetetraacetic acid into Fe2+-TauD are performed under an anaerobic environment to yield a binding equilibrium of 2400000 (Kd = 43 nM) and a DELTAG(0) value of -10.1 kcal/mol. Further analysis of the enthalpy/entropy contributions indicates a highly enthalpic binding event, where DELTAH = -11.6 kcal/mol. Investigations into the unfavorable entropy term leads to the observation of water molecules becoming organized within the Fe2+-TauD 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
Fe2+
nonheme Fe2+-dependent metalloenzyme. The metal-dependent active site in TauD is formed by two histidine and an aspartate side-chains coordinating to one face of the octahedral coordination geometry (2-His-1-carboxylate facial triad)
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
Fe2+
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview
Iron
comparative quantum mechanics/molecular mechanics and density functional theory calculations on the oxo-iron species. Protonation of the histidine ligands of iron is essential to reproduce the correct electronic representations of the enzyme. Enzyme is very efficient in reacting with substrates via low reaction barriers
Iron
-
ferrous active site, analysis by circular dichroism and magnetic circular dichroism. The excited-state splittings and energies of the two transitions of TauD/FeII are consistent with a distorted 6C resting ferrous site. One of the six ligands is weakly coordinated, and 2-oxoglutarate is bound in a bidentate fashion
Iron
-
upon binding Fe(II), anaerobic samples of wild-type TauD and the three active variants generate a weak green chromophore resembling a catecholate-FeI(III)species. The quione oxidation state of dihydroxyphenylalanine reacts with Fe(II) to form this species
additional information
-
Ni2+, Co2+, Mn2+, Cu2+, Zn2+, Mg2+, and Ca2+ have no stimulatory effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no reduction in enzyme activity is observed for sulfate concentrations up to 10 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
m6A mRNA Methylation Regulates Epithelial Innate Antimicrobial Defense Against Cryptosporidial Infection.
Neoplasms
ALKBH2 inhibition alleviates malignancy in colorectal cancer by regulating BMI1-mediated activation of NF-?B pathway.
Urinary Bladder Neoplasms
The tumor-suppressive effects of alpha-ketoglutarate-dependent dioxygenase FTO via N6-methyladenosine RNA methylation on bladder cancer patients.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic mechanism, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
real-time NMR spectra to follow enzymatic turnover
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.012
-
strain MC4100 grown in sulfate-free minimal medium containing 0.25 mM taurine as sulfur source
8.11
purified enzyme, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information