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Literature summary for 1.14.11.17 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
Search for more literature for 1.14.11.17

Protein Variants

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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