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
1.14.11.17
-
RECOMMENDED NAME
GeneOntology No.
taurine dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
-
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
mechanism
-
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
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
-
PATHWAY
KEGG Link
MetaCyc Link
Sulfur metabolism
-
Taurine and hypotaurine metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-aminoethanesulfonate dioxygenase
-
-
-
-
2-aminoethanesulfonic acid/alpha-ketoglutarate dioxygenase
-
-
alpha-ketoglutarate-dependent dioxygenase
-
-
alpha-ketoglutarate-dependent dioxygenase
Pseudomonas putida S-313
-
-
-
alpha-ketoglutarate-dependent taurine dioxygenase
-
-
-
-
AtsK
Pseudomonas putida S-313
-
-
-
Fe(II)/2-oxoglutarate-dependent taurine dioxygenase
-
-
Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase
-
-
Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase
Q88RA3
-
oxygenative alkylsulfatase
-
-
oxygenative alkylsulfatase
Pseudomonas putida S-313
-
-
-
SSI3
-
-
-
-
TauD
-
-
TauD
P37610
-
TauD
-
-
TauD
Q88RA3
-
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
P37610
-
taurine/2-oxoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate-dependent dioxygenase
-
-
taurine/alphaKG dioxygenase
-
-
taurine/alphaKGD
-
-
taurine: alpha-ketoglutarate dioxygenase
-
-
taurine:alpha-ketoglutarate dioxygenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
197809-75-9
-
297319-14-3
-
325506-70-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain MC4100
-
-
Manually annotated by BRENDA team
strain S-313
-
-
Manually annotated by BRENDA team
Pseudomonas putida S-313
strain S-313
-
-
Manually annotated by BRENDA team
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.485
-
1,3-dioxo-2-isoindolineenthanesulfonic acid
-
-
-
0.009
-
2-oxoglutarate
-
wild type enzyme, in the presence of taurine
0.011
-
2-oxoglutarate
-
-
0.012
-
2-oxoglutarate
-
mutant enzyme Y73I, in the presence of taurine
0.015
-
2-oxoglutarate
-
mutant enzyme Y73I, without taurine
0.02
-
2-oxoglutarate
-
wild type enzyme, without taurine
0.032
-
2-oxoglutarate
-
wild-type, 30C
0.048
-
2-oxoglutarate
-
mutant enzyme W98I, in the presence of taurine
0.055
-
2-oxoglutarate
-
mutant H255E, 30C
0.059
-
2-oxoglutarate
-
mutant H255Q, 30C
0.081
-
2-oxoglutarate
-
mutant D101E, 30C
1.49
-
butanesulfonic acid
-
-
1.51
-
hexanesulfonic acid
-
-
0.0051
-
N-methyltaurine
-
deuterated substrate
0.048
-
N-methyltaurine
-
commercially available substrate
0.054
-
N-methyltaurine
-
-
0.0056
-
O2
-
deuterated substrate 2-methyltaurine
0.041
-
O2
-
commercially available substrate 2-methyltaurine; substrate taurine
0.046
-
O2
-
substrate 2-methyltaurine
0.59
-
pentanesulfonic acid
-
-
0.019
-
Taurine
-
mutant H255E, 30C; wild-type, 30C
0.0194
-
Taurine
-
-
0.021
-
Taurine
-
mutant H255Q, 30C
0.052
-
Taurine
-
wild type enzyme
0.055
-
Taurine
-
-
0.061
-
Taurine
-
mutant D101E, 30C
0.145
-
MOPS
-
-
additional information
-
additional information
-
kinetic mechanism, overview
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00000001
-
O2
-
substrate 2-methyltaurine
14738
0.000000011
-
O2
-
deuterated substrate 2-methyltaurine
14738
0.000000012
-
O2
-
commercially available substrate 2-methyltaurine; sustrate taurine
14738
1.01
-
O2
-
-
14738
0.000000025
-
Taurine
-
-
16883
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.29
-
N-oxalylglycine
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0019
-
Co2+
-
IC50: 0.0019 mM, in the presence of Fe2+
0.041
-
Co2+
-
IC50: 0.041 mM
0.00071
-
Ni2+
-
IC50: 0.00071 mM, in the presence of Fe2+
0.032
-
Ni2+
-
IC50: 0.032 mM
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
assay at
PDB
SCOP
CATH
ORGANISM
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)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Trp128, Trp240, and Trp248 are hydroxylated upon exposure to oxygen
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
H99A
-
replacement of the residue that contributes the imidazole ligand cis to the oxo group. Density functional theory calculations show that the imidazole is replaced by a water ligand
H99A
-
no catalytic activity
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 ACCESSION NO.
COMMENTARY
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