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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
decarboxylation
-
-
dioxygenation
-
-
hydroxylation
-
the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
hydroxylation
-
catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II)
hydroxylation
-
-
hydroxylation
-
-
hydroxylation
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
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
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
cysteine metabolism
physiological function
-
nonheme iron enzyme, activation of C-H bonds
physiological function
-
important in antibiotic biosynthesis, oxygen sensing, DNA repair, biodegradation of anthropogenic compounds
additional information
-
development of a colorimetric assay method, based on the measurement of sulfite using Ellman's reagent, i.e. 2.5 mM 5,5'-dithiobis(2-nitrobenzoic acid), for determination of taurine in commercially available beverages and some biological samples, overview
additional information
-
metal-to-ligand charge-transfer transition involving the 2-oxoglutarate ligand with a six-coordinate metal center. Taurine does not coordinate the Fe(II) ion, but binds in its close vicinity, leading to loss of the coordinating water molecule. This change of the six-coordinate to five-coordinate Fe(II) center causes a small perturbation of the absorption spectrum
additional information
Q88RA3
metal-to-ligand charge-transfer transition involving the 2-oxoglutarate ligand with a six-coordinate metal center. Taurine does not coordinate the Fe(II) ion, but binds in its close vicinity, leading to loss of the coordinating water molecule. This change of the six-coordinate to five-coordinate Fe(II) center causes a small perturbation of the absorption spectrum
additional information
-
structure-activity analysis, modeling and simulations, overview. Modeling of TauD-(Fe-NO) complex and spectral analysis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Pseudomonas putida, Pseudomonas putida S-313
-
-
-
-
?
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
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
P37610
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
Q88RA3
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
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
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
P37610
enables the use of taurine as sulfur source
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
enables the use of taurine as sulfur source
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
reaction mechanism via two accumulating, kinetically competent intermediates upon reaction of the TauD:Fe(II):RKG:taurine complex with O2
-
-
?
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 + 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
-
-
?
MOPS + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
Pseudomonas putida, Pseudomonas putida S-313
-
the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
Q88RA3
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
P37610
enables the use of taurine as sulfur source
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
enables the use of taurine as sulfur source
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
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
Fe
-
catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II)
Fe2+
-
maximal activation between 0.005 and 0.150 mM
Fe2+
-
required, essential cofactor
Fe2+
-
required, bound in an open metal coordination site
Fe2+
-
required, forms iron-oxygen complex during the course of reaction
Fe2+
-
required for activity, highest activity in the presence of 0.1 mM
Fe2+
-
binding structure and role in the kinetic mechanism, overview
Fe2+
-
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview
Fe2+
Q88RA3
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview
Fe2+
-
dependent on, non-heme mononuclear Fe(II) center
Fe3+
-
formation of Fe3+-oxyl species as intermediates
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
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
additional information
-
Mg2+, Ca2+, Mn2+ or Ni2+ can not replace iron
additional information
-
Ni2+, Co2+, Mn2+, Cu2+, Zn2+, Mg2+, and Ca2+ have no stimulatory effect
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Co2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
Co2+
-
IC50: 0.0019 mM, in the presence of Fe2+; IC50: 0.041 mM
Cu2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
EDTA
-
complete inactivation
EDTA
-
0.1 mM EDTA abolishes activity completely
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
required for activity
ascorbate
-
50% increase in activity at 0.2-0.8 mM
ascorbate
-
3fold increase of activity at 0.2 mM
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.06
-
2-oxoglutarate
-
wild type enzyme, without taurine
0.12
-
2-oxoglutarate
-
mutant enzyme Y73I, without taurine
0.14
-
2-oxoglutarate
-
mutant enzyme W98I, in the presence of taurine
1
-
2-oxoglutarate
-
mutant enzyme Y73I, in the presence of taurine
0.74
-
Taurine
-
mutant D101E, 30C
1.1
-
Taurine
-
mutant H255E, 30C
2.7
-
Taurine
-
mutant H255Q, 30C
3
-
Taurine
-
wild type enzyme
3.3
-
Taurine
-
wild-type, 30C
3
-
2-oxoglutarate
-
wild type enzyme, in the presence of taurine
additional information
-
additional information
Q88RA3
real-time NMR spectra to follow enzymatic turnover
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
Q88RA3
purified enzyme, pH and temperature not specified in the publication
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2
-
-
assay at
6.2
-
-
assay at
7
-
-
in Tris-acetate buffer
7
-
-
assay at
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32000
-
-
-
32410
-
-
calculation from gene sequence
37400
-
-
estimated by SDS-PAGE
81000
-
-
gel filtration on Superose 6 and Superose 12 HR
110000
-
-
gel filtration
112000
-
Q88RA3
gel filtration
120000
-
Q88RA3
sedimentation velocity analytical ultracentrifugation
121000
-
-
gel filtration
127000
-
-
sedimentation velocity analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 37400, SDS-PAGE
dimer
-
crystal structure analysis
homotetramer
-
4 * 30250, gel filtration; 4 * 32000, SDS-PAGE
tetramer
-
4 * 32000, about, sequence calculation, TauDEc is a tetramer in solution and in the crystals, gel filtration and sedimentation velocity analytical ultracentrifugation
tetramer
Q88RA3
4 * 31000, about, sequence calculation, TauDPp is a tetramer in solution and in the crystals
homotetramer
Pseudomonas putida S-313
-
4 * 30250, gel filtration; 4 * 32000, SDS-PAGE
-
additional information
-
Geometric Structure of TauD-{FeNO}7, overview
additional information
Q88RA3
topology of an apo-TauDPp monomer,overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Trp128, Trp240, and Trp248 are hydroxylated upon exposure to oxygen
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
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
-
enzyme with bound substrate taurine, crystal structure analysis at 2.5 A resolution
-
hanging drop method, inclusion of taurine and 2-oxoglutarate is absolutely required for crystal formation
-
presence of taurine is required for crystal growth
-
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
Q88RA3
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DEAE-Sepharose column chromatography and HP phenyl-Sepharose column chromatography
-
dialysis against 25 mM Tris buffer at pH 8.0
-
recombinant His-tagged TauD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant protein using His-tag
-
two-step purification from overexpressing Escherichia coli to apparent homogeneity
-
Resource-Q anion-exchange column chromatography and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli as His-tag fusion protein
-
expression of His-tagged TauD in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of TauD in Escherichia coli strains BL21(DE3) and Rosetta Blue(DE3)
Q88RA3
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