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Literature summary extracted from

  • 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 (2007), J. Inorg. Biochem., 101, 797-808.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.17 D101A no catalytic activity Escherichia coli
1.14.11.17 D101C no catalytic activity Escherichia coli
1.14.11.17 D101E about 3-fold increase in Km values Escherichia coli
1.14.11.17 D101H no catalytic activity Escherichia coli
1.14.11.17 D101N no catalytic activity Escherichia coli
1.14.11.17 D101Q no catalytic activity Escherichia coli
1.14.11.17 H255A no catalytic activity Escherichia coli
1.14.11.17 H255C no catalytic activity Escherichia coli
1.14.11.17 H255D no catalytic activity Escherichia coli
1.14.11.17 H255E about 2-fold increase in Km value of 2-oxoglutarate Escherichia coli
1.14.11.17 H255N no catalytic activity Escherichia coli
1.14.11.17 H255Q about 2-fold increase in Km value of 2-oxoglutarate Escherichia coli
1.14.11.17 H99A no catalytic activity Escherichia coli
1.14.11.17 H99C no catalytic activity Escherichia coli
1.14.11.17 H99D no catalytic activity Escherichia coli
1.14.11.17 H99E no catalytic activity Escherichia coli
1.14.11.17 H99N no catalytic activity Escherichia coli
1.14.11.17 H99Q no catalytic activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.17 0.019
-
 taurine mutant H255E, 30°C Escherichia coli
1.14.11.17 0.019
-
 taurine wild-type, 30°C Escherichia coli
1.14.11.17 0.021
-
 taurine mutant H255Q, 30°C Escherichia coli
1.14.11.17 0.032
-
 2-oxoglutarate wild-type, 30°C Escherichia coli
1.14.11.17 0.055
-
 2-oxoglutarate mutant H255E, 30°C Escherichia coli
1.14.11.17 0.059
-
 2-oxoglutarate mutant H255Q, 30°C Escherichia coli
1.14.11.17 0.061
-
 taurine mutant D101E, 30°C Escherichia coli
1.14.11.17 0.081
-
 2-oxoglutarate mutant D101E, 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.17 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 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.17 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.17 taurine + 2-oxoglutarate + O2
-
 Escherichia coli sulfite + aminoacetaldehyde + succinate + CO2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.11.17 0.74
-
 taurine mutant D101E, 30°C Escherichia coli
1.14.11.17 1.1
-
 taurine mutant H255E, 30°C Escherichia coli
1.14.11.17 2.7
-
 taurine mutant H255Q, 30°C Escherichia coli
1.14.11.17 3.3
-
 taurine wild-type, 30°C Escherichia coli