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1,3-dioxo-2-isoindolineethanesulfonic acid + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
-
-
-
-
?
2-oxoglutarate + 2-methylaminoethane-1-sulfonic acid + O2
methylaminoacetaldehyde + succinate + sulfite + CO2
assay at pH 6.2, 30°C
-
-
?
4-aminobutyric acid + 2-oxoglutarate + O2
D-2-hydroxy-4-aminobutyric acid + succinate + CO2
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
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
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
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
beta-alanine + 2-oxoglutarate + O2
D-isoserine + succinate + CO2
activity with mutant enzyme F206Y is 2.4fold higher than activity with wild-type enzyme
-
-
?
butanesulfonic acid + 2-oxoglutarate + O2
sulfite + butanal + succinate + CO2
-
-
-
-
?
butyric acid + 2-oxoglutarate + O2
2-hydroxybutyric acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
hexanesulfonic acid + 2-oxoglutarate + O2
sulfite + hexanal + succinate + CO2
-
-
-
-
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
MOPS + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
-
-
-
-
?
N-methyltaurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + methylaminoacetaldehyde
-
-
-
-
?
O2 + 2-oxoglutarate + taurine
?
-
assay at pH 6.2, 30°C
-
-
?
pentanesulfonic acid + 2-oxoglutarate + O2
sulfite + pentanal + succinate + CO2
-
-
-
-
?
propionic acid + 2-oxoglutarate + O2
2-hydroxypropionic acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
taurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + aminoacetaldehyde
-
-
-
-
?
taurine + 2-oxoglutarate + O2
succinate + CO2 + 2-aminoethanal + sulfite
-
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
taurine + alpha-ketoadipate + O2
sulfite + aminoacetaldehyde + pentan-1,5-dioic acid + CO2
-
alpha-ketoadipate is less active than 2-oxoglutarate, no activity with pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketocaproate, alpha-ketoisovalerate and oxalacetat
-
-
?
valeric acid + 2-oxoglutarate + O2
2-hydroxyvaleric acid + succinate + CO2
mutant enzyme F206Y shows low activity. No activity with the wild-type enzyme
-
-
?
additional information
?
-
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
-
-
-
-
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
-
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
658130, 658975, 658984, 671301, 671717, 673443, 674930, 688192, 712249, 723940, 724974, 725787 -
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
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
-
enables the use of taurine as sulfur source
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
enables the use of taurine as sulfur source
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
enables the use of taurine as sulfur source
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
reaction mechanism via two accumulating, kinetically competent intermediates upon reaction of the TauD:Fe(II):RKG:taurine complex with O2
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
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
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
-
-
-
?
additional information
?
-
-
the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
-
-
?
additional information
?
-
-
the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
-
-
?
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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
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
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+
-
-
Fe2+
-
maximal activation between 0.005 and 0.150 mM
Fe2+
-
required, bound in an open metal coordination site
Fe2+
required, essential cofactor
Fe2+
-
required, forms iron-oxygen complex during the course of reaction
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+
-
dependent on, non-heme mononuclear Fe(II) center
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+
-
required for activity, highest activity in the presence of 0.1 mM
Fe2+
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview
Iron
-
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
-
Mg2+, Ca2+, Mn2+ or Ni2+ can not replace iron
additional information
-
Ni2+, Co2+, Mn2+, Cu2+, Zn2+, Mg2+, and Ca2+ have no stimulatory effect
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
-
brenda
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
brenda
Kahnert, A.; Kertesz, M.A.
Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313
J. Biol. Chem.
275
31661-31667
2000
Pseudomonas putida, Pseudomonas putida S-313
brenda
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)
brenda
Grzyska, P.K.; Hausinger, R.P.
Cr(II) reactivity of taurine/alpha-ketoglutarate dioxygenase
Inorg. Chem.
46
10087-10092
2007
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
de Visser, S.
Elucidating enzyme mechanism and intrinsic chemical properties of short-lived intermediates in the catalytic cycles of cysteine dioxygenase and taurine/alpha-ketoglutarate dioxygenase
Coord. Chem. Rev.
253
754-768
2009
Homo sapiens
-
brenda
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)
brenda
Mirica, L.M.; McCusker, K.P.; Munos, J.W.; Liu, H.W.; Klinman, J.P.
18O kinetic isotope effects in non-heme iron enzymes: probing the nature of Fe/O2 intermediates
J. Am. Chem. Soc.
130
8122-8123
2008
Bacteria
brenda
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)
brenda
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
-
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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)
-
brenda
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
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54
2278-2283
2015
Escherichia coli (P37610)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda