Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.14.11.17: taurine dioxygenase

This is an abbreviated version!
For detailed information about taurine dioxygenase, go to the full flat file.

Word Map on EC 1.14.11.17

Reaction

taurine
+
2-oxoglutarate
+
O2
=
sulfite
+
aminoacetaldehyde
+
succinate
+
CO2

Synonyms

2-aminoethanesulfonate dioxygenase, 2-aminoethanesulfonic acid/alpha-ketoglutarate dioxygenase, alpha-ketoglutarate-dependent dioxygenase, alpha-ketoglutarate-dependent taurine dioxygenase, alpha-ketoglutarate/taurine dioxygenase, AtsK, Fe(II)/2-oxoglutarate-dependent taurine dioxygenase, Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase, oxygenative alkylsulfatase, SSI3, TauD, 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, taurine/2-oxoglutarate dioxygenase, taurine/alpha-ketoglutarate dioxygenase, taurine/alpha-ketoglutarate-dependent dioxygenase, taurine/alphaKG dioxygenase, taurine/alphaKGD, taurine: alpha-ketoglutarate dioxygenase, taurine:2OG dioxygenase, taurine:alpha-ketoglutarate dioxygenase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.17 taurine dioxygenase

Engineering

Engineering on EC 1.14.11.17 - taurine dioxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
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
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
-
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
-