Information on EC 1.14.11.17 - taurine dioxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.11.17
-
RECOMMENDED NAME
GeneOntology No.
taurine dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
dioxygenation
-
-
hydroxylation
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Sulfur metabolism
-
-
Taurine and hypotaurine metabolism
-
-
taurine degradation
-
-
taurine degradation IV
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
197809-75-9
-
297319-14-3
-
325506-70-5
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-dioxo-2-isoindolineenthanesulfonic acid + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + 2-methylaminoethane-1-sulfonic acid + O2
methylaminoacetaldehyde + succinate + sulfite + CO2
show the reaction diagram
-
assay at pH 6.2, 30C
-
-
?
butanesulfonic acid + 2-oxoglutarate + O2
sulfite + butanal + succinate + CO2
show the reaction diagram
-
-
-
-
?
hexanesulfonic acid + 2-oxoglutarate + O2
sulfite + hexanal + succinate + CO2
show the reaction diagram
-
-
-
-
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
show the reaction diagram
MOPS + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
show the reaction diagram
-
-
-
-
?
N-methyltaurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + methylaminoacetaldehyde
show the reaction diagram
-
-
-
-
?
O2 + 2-oxoglutarate + taurine
?
show the reaction diagram
-
assay at pH 6.2, 30C
-
-
?
pentanesulfonic acid + 2-oxoglutarate + O2
sulfite + pentanal + succinate + CO2
show the reaction diagram
-
-
-
-
?
taurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + aminoacetaldehyde
show the reaction diagram
-
-
-
-
?
taurine + 2-oxoglutarate + O2
succinate + CO2 + aminoethanol + sulfite
show the reaction diagram
-
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
taurine + alpha-ketoadipate + O2
sulfite + aminoacetaldehyde + pentan-1,5-dioic acid + CO2
show the reaction diagram
-
alpha-ketoadipate is less active than 2-oxoglutarate, no activity with pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketocaproate, alpha-ketoisovalerate and oxalacetat
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Fe3+
-
formation of Fe3+-oxyl species as intermediates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
N-oxalylglycine
-
-
Ni2+
-
IC50: 0.00071 mM, in the presence of Fe2+; IC50: 0.032 mM
nonyl sulfate
-
inhibits at concentrations between 1 and 10 mM
SDS
-
inhibits at concentrations between 1 and 10 mM
Zn2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
additional information
-
no reduction in enzyme activity is observed for sulfate concentrations up to 10 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
required for activity
ascorbate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.485
1,3-dioxo-2-isoindolineenthanesulfonic acid
-
-
-
0.009 - 0.081
2-oxoglutarate
1.49
butanesulfonic acid
-
-
1.51
hexanesulfonic acid
-
-
0.145
MOPS
-
-
0.0051 - 0.054
N-methyltaurine
0.0056 - 0.046
O2
0.59
pentanesulfonic acid
-
-
0.019 - 0.061
taurine
additional information
additional information
-
kinetic mechanism, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 3
2-oxoglutarate
0.74 - 3.3
taurine
additional information
additional information
Pseudomonas putida
Q88RA3
real-time NMR spectra to follow enzymatic turnover
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000001 - 1.01
O2
0.000000025
taurine
Escherichia coli
-
-
595
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
N-oxalylglycine
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019 - 0.041
Co2+
0.00071 - 0.032
Ni2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
strain MC4100 grown in sulfate-free minimal medium containing 0.25 mM taurine as sulfur source
1.64
-
purified enzyme
3.56
-
purified enzyme, pH and temperature not specified in the publication
8.11
purified enzyme, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium avium (strain 104)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Pseudomonas putida (strain KT2440)
Pseudomonas putida (strain KT2440)
Pseudomonas putida (strain KT2440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32410
-
calculation from gene sequence
37400
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estimated by SDS-PAGE
81000
-
gel filtration on Superose 6 and Superose 12 HR
110000
-
gel filtration
112000
gel filtration
120000
sedimentation velocity analytical ultracentrifugation
121000
-
gel filtration
127000
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sedimentation velocity analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Trp128, Trp240, and Trp248 are hydroxylated upon exposure to oxygen
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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density functional theory calculations based on a series of models for the key intermediate with the Fe(IV) ion coordinated by the expected two imidazoles from His99 and His255, two carboxylates, succinate and Asp101, and oxo ligands. Calculated parameters of distorted octahedral models for the intermediate, in which one of the carboxylates serves as a monodentate ligand and the other as a bidentate ligand, and a trigonal bipyramidal model, in which both carboxylates serve as monodentate ligands, agree well with the experimental parameters
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electron spin echo-detected EPR spectrum ESE and deuterium electron spin echo envelope modulation spectrum ESEEM of the Fe(II)-NO form of the enzyme treated with 2-oxoglutarate and taurine
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enzyme with bound substrate taurine, crystal structure analysis at 2.5 A resolution
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hanging drop method, inclusion of taurine and 2-oxoglutarate is absolutely required for crystal formation
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presence of taurine is required for crystal growth
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three crystal structures of the apo form, vapor diffusion techniques, protein solution contains 1. 27-28 m/ml TauDPp in 25 mM Tris-HCl, pH 7.7, or 2. 21 mg/ml TauDPp in 25 mM Tris-HCl pH 7.7, containing 10 mM taurine, 0.1 M (NH4)2SO4 and 20% v?v glycerol, mixed with reservoir solution containing 1. 15% w?v PEG 1000, 40% v?v PEG 400, 0.15 M NaK phosphate, and 0.1 M imidazole chloride, pH 6.5, or 2. 20% w?v PEG 5000 monomethyl ether, 0.1 M Bis-Tris-HCl, pH 6.5, X-ray diffraction structure determination and analysis at 1.85-2.6 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
incubation at 30C leads to rapid inactivation, effect is enhanced by ascorbate and not due to oxidation of the enzyme-bound ferrous iron
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, phosphate buffer, 16% glycerol, 10 weeks, activity increases 4-fold
-
-20C, phosphate buffer, without glycerol, 3 weeks, more than 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and HP phenyl-Sepharose column chromatography
-
dialysis against 25 mM Tris buffer at pH 8.0
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recombinant His-tagged TauD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant protein using His-tag
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Resource-Q anion-exchange column chromatography and Superdex 200 gel filtration
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two-step purification from overexpressing Escherichia coli to apparent homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tag fusion protein
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of His-tagged TauD in Escherichia coli strain BL21(DE3)
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expression of TauD in Escherichia coli strains BL21(DE3) and Rosetta Blue(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101A
-
no catalytic activity
D101C
-
no catalytic activity
D101E
-
about 3-fold increase in Km values
D101H
-
no catalytic activity
D101N
-
no catalytic activity
D101Q
-
no catalytic activity
F159A
-
decrease in coupling of oxygen activation to C-H cleavage
F159G
-
decrease in coupling of oxygen activation to C-H cleavage
F159L
-
decrease in coupling of oxygen activation to C-H cleavage
F159V
-
decrease in coupling of oxygen activation to C-H cleavage
H255A
-
no catalytic activity
H255C
-
no catalytic activity
H255D
-
no catalytic activity
H255E
-
about 2-fold increase in Km value of 2-oxoglutarate
H255N
-
no catalytic activity
H255Q
-
about 2-fold increase in Km value of 2-oxoglutarate
H99C
-
no catalytic activity
H99D
-
no catalytic activity
H99E
-
no catalytic activity
H99N
-
no catalytic activity
H99Q
-
no catalytic activity
W98I
-
reduced activity compared to the wild type enzyme
Y73F
-
active, but mutant is incapable of formation of a Cr(III)-semiquinone chromophore
Y73I
-
reduced activity compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
development of a colorimetric assay method for determination of taurine in commercially available beverages and some biological samples using the taurine dioxygenase. Taurine determination in food control, biological research, and diagnoses based on urinary taurine concentration
biotechnology
-
model system for non-heme iron oxygenases
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