3.6.1.39: thymidine-triphosphatase
This is an abbreviated version!
For detailed information about thymidine-triphosphatase, go to the full flat file.
Word Map on EC 3.6.1.39
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3.6.1.39
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bacteriophage
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single-stranded
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strand
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primase
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unwind
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duplex
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fork
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hexamer
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oligoribonucleotides
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dna-dependent
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ring-shaped
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richardson
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helicase-primase
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primase-helicase
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tetraribonucleotides
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replisome
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template-directed
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okazaki
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rna-primed
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dnab
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medicine
- 3.6.1.39
- bacteriophage
-
single-stranded
- strand
- primase
-
unwind
- duplex
- fork
-
hexamer
- oligoribonucleotides
-
dna-dependent
-
ring-shaped
-
richardson
-
helicase-primase
-
primase-helicase
-
tetraribonucleotides
-
replisome
-
template-directed
-
okazaki
-
rna-primed
- dnab
- medicine
Reaction
Synonyms
desoxythymidine-5'-triphosphatase, dTTPase, dTTPase-dUTPase, gene 4 protein, Gp4, T7 DNA helicase, T7 helicase, thymidine triphosphate nucleotidohydrolase
ECTree
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Engineering
Engineering on EC 3.6.1.39 - thymidine-triphosphatase
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E343Q
N468A
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the mutant hydrolyzes dTTP at rates comparable with wild type enzyme. N468A hydrolyzes nearly 4fold less efficiently than the wild type enzyme in the absence of single-stranded DNA and is not stimulated by the presence of single-stranded DNA
R493A/N468A
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the mutant hydrolyzes dTTP at rates comparable with wild type enzyme and is not stimulated by the presence of single-stranded DNA
R493Q
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site-directed mutagenesis, the mutant is inactive, dTTP hydrolysis and DNA unwinding activities are abolished, but the mutant shows increased single-stranded DNA binding affinity compared to the wild-type enzyme, overview
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the mutant hydrolyzes dTTP at rates comparable with wild type enzyme and is not stimulated by the presence of single-stranded DNA
R493Q
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the mutant maintains only the basal level of dTTPase activity but does not exhibit activation in the dTTP hydrolysis activity in the presence of single-stranded DNA