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1.14.11.6: thymine dioxygenase

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

Word Map on EC 1.14.11.6

Reaction

thymine
+
2-oxoglutarate
 +
O2
=
5-Hydroxymethyluracil
 +
succinate
 +
CO2

Synonyms

5-hydroxy-methyluracil dioxygenase, 5-hydroxy-methyluracil oxygenase, EC 1.14.11.5, Fe2+/2-oxoglutarate dependent hydroxylase, J binding protein 1, J binding protein 2, J-binding protein 1, J-binding protein 2, JBP1, JBP2, More, T7H, thymidine hydroxylase, thymine 7-hydroxylase, thymine dioxygenase, thymine hydroxylase, thymine-7-hydroxylase

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
                1.14.11.6 thymine dioxygenase

Engineering

Engineering on EC 1.14.11.6 - thymine dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D215S
-
mutant proteins fail to restore the J-level in the JBP1 null trypanosomes to wild-type levels
D416A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
H213S
-
mutant proteins fail to restore the J-level in the JBP1 null trypanosomes to wild-type levels
H414A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
H465A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
R478A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
V482A/L548Q
site-directed and random mutagenesis, the mutant can complement the JBP2 knockout mutant strain
D216N
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
E122A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
F292A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H214A
site-directed mutagenesis, the mutant shows highly reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
H271A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
L192A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
L223A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
N294A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
N87A
site-directed mutagenesis, the mutant shows similar activity with thymine and altered substrate specificity compared to the wild-type enzyme
R190A
site-directed mutagenesis, the mutant shows highly reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
R190K
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
R286A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
R286K
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
S288A
site-directed mutagenesis, the mutant shows similar activity with thymine and altered substrate specificity compared to the wild-type enzyme
V273A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Y194F
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Y217A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y217F
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
N187D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N250D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N293D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R285C
site-directed mutagenesis, inactive active site mutant
D191A
-
mutation abrogates the ability of JBP1 to complement JBP1 null mutants
D393A
site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2 inside the catalytic domain
H189A
-
mutation abrogates the ability of JBP1 to complement JBP1 null mutants
H189A/D191A
-
mutation abrogates the ability of JBP1 to complement JBP1 null mutants
H239A
-
mutation abrogates the ability of JBP1 to complement JBP1 null mutants
H391A
site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2, expression of the TH mutant H319A fails to stimulate base J formation
H441A
site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2 inside the catalytic domain
R255A
-
mutation abrogates the ability of JBP1 to complement JBP1 null mutants
R445A
site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2 inside the catalytic domain
V259A
-
mutation abrogates the ability of JBP1 to complement JBP1 null mutants
V459A
site-directed mutagenesis, control substitution of a residue outside the catalytic domain
additional information