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Information on EC 1.14.11.17 - taurine dioxygenase and Organism(s) Escherichia coli and UniProt Accession P37610

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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.
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This record set is specific for:
Escherichia coli
UNIPROT: P37610
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-ketoglutarate/taurine dioxygenase
-
taurine alpha-ketoglutarate dioxygenase
-
taurine-alpha-ketoglutarate dioxygenase
-
taurine/alpha-ketoglutarate dioxygenase
-
taurine/alphaKGD
-
taurine:2OG dioxygenase
-
2-aminoethanesulfonate dioxygenase
-
-
-
-
2-aminoethanesulfonic acid/alpha-ketoglutarate dioxygenase
-
-
alpha-ketoglutarate-dependent taurine dioxygenase
-
-
-
-
Fe(II)/2-oxoglutarate-dependent taurine dioxygenase
-
-
Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase
-
-
SSI3
-
-
-
-
TauD-{FeNO}7
-
-
taurine (2-aminoethanesulfonate)/2-oxoglutarate dioxygenase
-
-
taurine alpha ketoglutarate dioxygenase
-
-
taurine hydroxylase
-
-
taurine/2-oxoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate-dependent dioxygenase
-
-
taurine/alphaKG dioxygenase
-
-
taurine: alpha-ketoglutarate dioxygenase
-
-
taurine:alpha-ketoglutarate dioxygenase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
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
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
decarboxylation
-
the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
hydroxylation
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + 2-methylaminoethane-1-sulfonic acid + O2
methylaminoacetaldehyde + succinate + sulfite + CO2
show the reaction diagram
assay at pH 6.2, 30°C
-
-
?
4-aminobutyric acid + 2-oxoglutarate + O2
D-2-hydroxy-4-aminobutyric acid + succinate + CO2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
beta-alanine + 2-oxoglutarate + O2
D-isoserine + succinate + CO2
show the reaction diagram
activity with mutant enzyme F206Y is 2.4fold higher than activity with wild-type enzyme
-
-
?
butyric acid + 2-oxoglutarate + O2
2-hydroxybutyric acid + succinate + CO2
show the reaction diagram
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
propionic acid + 2-oxoglutarate + O2
2-hydroxypropionic acid + succinate + CO2
show the reaction diagram
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
valeric acid + 2-oxoglutarate + O2
2-hydroxyvaleric acid + succinate + CO2
show the reaction diagram
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
1,3-dioxo-2-isoindolineethanesulfonic acid + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
MOPS + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
show the reaction diagram
-
-
-
-
?
N-methyltaurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + methylaminoacetaldehyde
show the reaction diagram
-
-
-
-
?
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
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
Fe3+
formation of Fe3+-oxyl species as intermediates
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
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
-
catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II)
additional information
-
Mg2+, Ca2+, Mn2+ or Ni2+ can not replace iron
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
N-oxalylglycine
-
-
Zn2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
50% increase in activity at 0.2-0.8 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.485
1,3-dioxo-2-isoindolineethanesulfonic 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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000001 - 0.000000012
O2
0.000000025
taurine
-
-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological function
-
important in antibiotic biosynthesis, oxygen sensing, DNA repair, biodegradation of anthropogenic compounds
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
gel filtration
127000
-
sedimentation velocity analytical ultracentrifugation
32000
32410
-
calculation from gene sequence
37400
-
estimated by SDS-PAGE
81000
-
gel filtration on Superose 6 and Superose 12 HR
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dimer
-
2 * 37400, 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
additional information
-
Geometric Structure of TauD-{FeNO}7, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
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
hanging drop method, inclusion of taurine and 2-oxoglutarate is absolutely required for crystal formation
hanging drop vapor diffusion method, crystals of Escherichia coli TauD are grown in the presence of vanadyl, taurine, and the coproduct succinate yield a 1.73 A resolution structure containing two molecules in the asymmetric unit
presence of taurine is required for crystal growth
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
-
enzyme with bound substrate taurine, crystal structure analysis at 2.5 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101Q
the variant suppress the conformational change, supporting the involvement in the structural rearrangement. The initial reduction E1/2 in D101Q TauD decreases by 50 mV relative to the wild-type enzyme, reaching comparable values at the end of the reduction. While the initial exponential phase of the oxidationof D101Q is very similar to that of the wild-type protein, oxidation does not continue beyond 100 s
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
F206Y
the conversions of the improved catalyst increases by at least 140% compared to that of the wild-type enzyme and shows broadened substrate scope
H255Q
the variant suppress the conformational change, supporting the involvement in the structural rearrangement. Both the reduction and oxidation E1/2 are lower in H255Q TauD than in wild-type enzyme, with no noticeable oxidative reorganization. The reductive reorganization for this protein reaches saturation after 1200 s
H99A
the variant shows a larg net redox change relative to the wild-type protein, suggesting that redox-coupled protonation of H99 is required for high redox potentials of the metal
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
incubation at 30°C 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
-20°C, phosphate buffer, 16% glycerol, 10 weeks, activity increases 4-fold
-
-20°C, phosphate buffer, without glycerol, 3 weeks, more than 50% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein using His-tag
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
-
two-step purification from overexpressing Escherichia coli to apparent homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tag fusion protein
expression in Escherichia coli BL21(DE3)
overexpression in BL21(DE3) Escherichia coli
overexpression in Escherichia coli BL21(DE3) cells harboring plasmid pME4141
expression of His-tagged TauD in Escherichia coli strain BL21(DE3)
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eichhorn, E.; Van der Ploeg, J.R.; Kertesz, M.A.; Leisinger, T.
Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli
J. Biol. Chem.
272
23031-23036
1997
Escherichia coli
Manually annotated by BRENDA team
Elkins, J.M.; Ryle, M.J.; Clifton, I.J.; Dunning Hotopp, J.C.; Lloyd, J.S.; Burzlaff, N.I.; Baldwin, J.E.; Hausinger, R.P.; Roach, P.L.
X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates
Biochemistry
41
5185-5192
2002
Escherichia coli (P37610), Escherichia coli
Manually annotated by BRENDA team
O'Brien, J.R.; Schuller, D.J.; Yang, V.S.; Dillard, B.D.; Lanzilotta, W.N.
Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure
Biochemistry
42
5547-5554
2003
Escherichia coli (P37610), Escherichia coli
Manually annotated by BRENDA team
Price, J.C.; Barr, E.W.; Hoffart, L.M.; Krebs, C.; Bollinger, J.M., Jr.
Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli
Biochemistry
44
8138-8147
2005
Escherichia coli
Manually annotated by BRENDA team
Proshlyakov, D.A.; Henshaw, T.F.; Monterosso, G.R.; Ryle, M.J.; Hausinger, R.P.
Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase
J. Am. Chem. Soc.
126
1022-1023
2004
Escherichia coli
Manually annotated by BRENDA team
Riggs-Gelasco, P.J.; Price, J.C.; Guyer, R.B.; Brehm, J.H.; Barr, E.W.; Bollinger, J.M., Jr.; Krebs, C.
EXAFS spectroscopic evidence for an Fe:O Unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase
J. Am. Chem. Soc.
126
8108-8109
2004
Escherichia coli
Manually annotated by BRENDA team
Luo, L.; Pappalardi, M.B.; Tummino, P.J.; Copeland, R.A.; Fraser, M.E.; Grzyska, P.K.; Hausinger, R.P.
An assay for Fe(II)/2-oxoglutarate-dependent dioxygenases by enzyme-coupled detection of succinate formation
Anal. Biochem.
353
69-74
2006
Escherichia coli
Manually annotated by BRENDA team
Kalliri, E.; Grzyska, P.K.; Hausinger, R.P.
Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/alpha-ketoglutarate dioxygenase, TauD
Biochem. Biophys. Res. Commun.
338
191-197
2005
Escherichia coli
Manually annotated by BRENDA team
de Visser, S.P.
Can the peroxosuccinate complex in the catalytic cycle of taurine/alpha-ketoglutarate dioxygenase (TauD) act as an alternative oxidant?
Chem. Commun. (Camb. )
2007
171-173
2007
Escherichia coli (P37610)
Manually annotated by BRENDA team
Bollinger, J.M.; Price, J.C.; Hoffart, L.M.; Barr, E.W.; Krebs, C.
Mechanism of taurine: alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli
Eur. J. Inorg. Chem.
2005
4245-4254
2005
Escherichia coli
-
Manually annotated by BRENDA team
Koehntop, K.D.; Marimanikkuppam, S.; Ryle, M.J.; Hausinger, R.P.; Que, L.
Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism
J. Biol. Inorg. Chem.
11
63-72
2006
Escherichia coli
Manually annotated by BRENDA team
Muthukumaran, R.B.; Grzyska, P.K.; Hausinger, R.P.; McCracken, J.
Probing the iron-substrate orientation for taurine/alpha-ketoglutarate dioxygenase using deuterium electron spin echo envelope modulation spectroscopy
Biochemistry
46
5951-5959
2007
Escherichia coli (P37610)
Manually annotated by BRENDA team
Grzyska, P.K.; Hausinger, R.P.
Cr(II) reactivity of taurine/alpha-ketoglutarate dioxygenase
Inorg. Chem.
46
10087-10092
2007
Escherichia coli
Manually annotated by BRENDA team
Neidig, M.L.; Brown, C.D.; Light, K.M.; Fujimori, D.G.; Nolan, E.M.; Price, J.C.; Barr, E.W.; Bollinger, J.M.; Krebs, C.; Walsh, C.T.; Solomon, E.I.
CD and MCD of CytC3 and taurine dioxygenase: role of the facial triad in alpha-KG-dependent oxygenases
J. Am. Chem. Soc.
129
14224-14231
2007
Escherichia coli
Manually annotated by BRENDA team
Sinnecker, S.; Svensen, N.; Barr, E.W.; Ye, S.; Bollinger, J.M.; Neese, F.; Krebs, C.
Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant
J. Am. Chem. Soc.
129
6168-6179
2007
Escherichia coli
Manually annotated by BRENDA team
Grzyska, P.K.; Mueller, T.A.; Campbell, M.G.; Hausinger, R.P.
Metal ligand substitution and evidence for quinone formation in taurine/alpha-ketoglutarate dioxygenase
J. Inorg. Biochem.
101
797-808
2007
Escherichia coli
Manually annotated by BRENDA team
Godfrey, E.; Porro, C.S.; de Visser, S.P.
Comparative quantum mechanics/molecular mechanics (QM/MM) and density functional theory calculations on the oxo-iron species of taurine/alpha-ketoglutarate dioxygenase
J. Phys. Chem. A
112
2464-2468
2008
Escherichia coli (P37610)
Manually annotated by BRENDA team
Ye, S.; Neese, F.
Quantum chemical studies of C-H activation reactions by high-valent nonheme iron centers
Curr. Opin. Chem. Biol.
13
89-98
2009
Escherichia coli (P37610)
Manually annotated by BRENDA team
McCusker, K.P.; Klinman, J.P.
Modular behavior of tauD provides insight into the origin of specificity in alpha-ketoglutarate-dependent nonheme iron oxygenases
Proc. Natl. Acad. Sci. USA
106
19791-19795
2009
Escherichia coli (P37610)
Manually annotated by BRENDA team
McCusker, K.; Klinman, J.
Facile synthesis of 1,1-[2H2]-2-methylaminoethane-1-sulfonic acid as a substrate for taurine a ketoglutarate dioxygenase (TauD)
Tetrahedron Lett.
50
611-613
2009
Escherichia coli
-
Manually annotated by BRENDA team
Ye, S.; Price, J.C.; Barr, E.W.; Green, M.T.; Bollinger, J.M.; Krebs, C.; Neese, F.
Cryoreduction of the NO-adduct of taurine:alpha-ketoglutarate dioxygenase (TauD) yields an elusive {FeNO}(8) species
J. Am. Chem. Soc.
132
4739-4751
2010
Escherichia coli
Manually annotated by BRENDA team
Matsuda, M.; Asano, Y.
A simple assay of taurine concentrations in food and biological samples using taurine dioxygenase
Anal. Biochem.
427
121-123
2012
Escherichia coli
Manually annotated by BRENDA team
Knauer, S.H.; Hartl-Spiegelhauer, O.; Schwarzinger, S.; Haenzelmann, P.; Dobbek, H.
The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers
FEBS J.
279
816-831
2012
Escherichia coli, Pseudomonas putida (Q88RA3), Pseudomonas putida KT 2240 (Q88RA3)
Manually annotated by BRENDA team
Casey, T.M.; Grzyska, P.K.; Hausinger, R.P.; McCracken, J.
Measuring the orientation of taurine in the active site of the non-heme Fe(II)/alpha-ketoglutarate-dependent taurine hydroxylase (TauD) using electron spin echo envelope modulation (ESEEM) spectroscopy
J. Phys. Chem. B
117
10384-10394
2013
Escherichia coli
Manually annotated by BRENDA team
Wetzl, D.; Bolsinger, J.; Nestl, B.; Hauer, B.
alpha-Hydroxylation of carboxylic acids catalyzed by taurine dioxygenase
ChemCatChem
8
1361-1366
2016
Escherichia coli (P37610)
-
Manually annotated by BRENDA team
Henderson, K.L.; Mueller, T.A.; Hausinger, R.P.; Emerson, J.P.
Calorimetric assessment of Fe(2+) binding to ?-ketoglutarate/taurine dioxygenase ironing out the energetics of metal coordination by the 2-His-1-carboxylate facial triad
Inorg. Chem.
54
2278-2283
2015
Escherichia coli (P37610)
Manually annotated by BRENDA team
Alvarez-Barcia, S.; Kaestner, J.
Atom tunneling in the hydroxylation process of taurine/alpha-ketoglutarate dioxygenase identified by quantum mechanics/molecular mechanics simulations
J. Phys. Chem. B
121
5347-5354
2017
Escherichia coli (P37610)
Manually annotated by BRENDA team
Davis, K.M.; Altmyer, M.; Martinie, R.J.; Schaperdoth, I.; Krebs, C.; Bollinger, J.M.; Boal, A.K.
Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD
Biochemistry
58
4218-4223
2019
Escherichia coli (P37610), Escherichia coli K12 (P37610)
Manually annotated by BRENDA team
Ali, H.S.; de Visser, S.P.
Electrostatic perturbations in the substrate-binding pocket of taurine/alpha-ketoglutarate dioxygenase determine its selectivity
Chemistry
28
e202104167
2022
Escherichia coli (P37610), Escherichia coli K12 (P37610)
Manually annotated by BRENDA team
John, C.W.; Hausinger, R.P.; Proshlyakov, D.A.
Structural origin of the large redox-linked reorganization in the 2-oxoglutarate dependent oxygenase, TauD
J. Am. Chem. Soc.
141
15318-15326
2019
Escherichia coli (P37610), Escherichia coli K12 (P37610)
Manually annotated by BRENDA team
Li, M.; Henderson, K.L.; Martinez, S.; Hausinger, R.P.; Emerson, J.P.
The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD)
J. Biol. Inorg. Chem.
23
785-793
2018
Escherichia coli (P37610), Escherichia coli K12 (P37610)
Manually annotated by BRENDA team
John, C.W.; Swain, G.M.; Hausinger, R.P.; Proshlyakov, D.A.
Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD
J. Phys. Chem. B
123
7785-7793
2019
Escherichia coli (P37610), Escherichia coli K12 (P37610)
Manually annotated by BRENDA team