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19
8-oxo-GTP
-
wild type enzyme, at 37°C, pH not specified in the publication
13
dCTP
-
wild type enzyme, at 37°C, pH not specified in the publication
94
5-methyl-CTP
-
wild type enzyme, at 37°C, pH not specified in the publication
210
5-methyl-CTP
-
wild type enzyme, at 37°C, pH not specified in the publication
1100
5-methyl-CTP
-
wild type enzyme, at 30°C, pH not specified in the publication
93
5-methyl-UTP
-
wild type enzyme, at 37°C, pH not specified in the publication
170
5-methyl-UTP
-
wild type enzyme, at 30°C, pH not specified in the publication
510
5-methyl-UTP
-
wild type enzyme, at 30°C, pH not specified in the publication
570
5-methyl-UTP
-
wild type enzyme, at 37°C, pH not specified in the publication
17
CTP
-
wild type enzyme, at 30°C, pH not specified in the publication
46
CTP
-
wild type enzyme, at 37°C, pH not specified in the publication
46
CTP
-
wild type enzyme, at 37°C, pH not specified in the publication
280
CTP
-
wild type enzyme, at 30°C, pH not specified in the publication
41.5
dITP
-
pH 9.0, 80°C
6100
dITP
-
pH 10.0, 75°C
21
dTTP
-
wild type enzyme, at 37°C, pH not specified in the publication
22
dTTP
-
mutant enzyme K82A, at 37°C, pH not specified in the publication
33
dTTP
-
mutant enzyme E188A, at 30°C, pH not specified in the publication
54
dTTP
-
mutant enzyme N77A, at 30°C, pH not specified in the publication
55
dTTP
-
mutant enzyme F193A, at 30°C, pH not specified in the publication
57
dTTP
-
mutant enzyme S10A, at 37°C, pH not specified in the publication
57
dTTP
-
mutant enzyme T26A, at 30°C, pH not specified in the publication
58
dTTP
-
mutant enzyme R23A, at 37°C, pH not specified in the publication
61
dTTP
-
mutant enzyme Q76A, at 30°C, pH not specified in the publication
79
dTTP
-
mutant enzyme K194A, at 30°C, pH not specified in the publication
120
dTTP
-
wild type enzyme, at 30°C, pH not specified in the publication
130
dTTP
-
mutant enzyme R12A, at 37°C, pH not specified in the publication
170
dTTP
-
mutant enzyme R29A, at 30°C, pH not specified in the publication
230
dTTP
-
wild type enzyme, at 30°C, pH not specified in the publication
290
dTTP
-
wild type enzyme, at 37°C, pH not specified in the publication
27.2
ITP
-
pH 9.0, 80°C
130
pseudo-UTP
-
wild type enzyme, at 37°C, pH not specified in the publication
220
pseudo-UTP
-
wild type enzyme, at 37°C, pH not specified in the publication
270
pseudo-UTP
-
wild type enzyme, at 30°C, pH not specified in the publication
1300
pseudo-UTP
-
wild type enzyme, at 30°C, pH not specified in the publication
17
UTP
-
wild type enzyme, at 37°C, pH not specified in the publication
68
UTP
-
wild type enzyme, at 30°C, pH not specified in the publication
88
UTP
-
wild type enzyme, at 30°C, pH not specified in the publication
220
UTP
-
wild type enzyme, at 37°C, pH not specified in the publication
13.1
XTP
-
pH 9.0, 80°C
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malfunction
-
ITPA deficiency causes disruption of the sarcomeric structure and dysfunction of car-diomyocytes. Itpa-deficient mice exhibit peri-orpostnatal lethality dependent on the genetic background. The heart of the Itpa-deficient mouse is structurally and functionally abnormal. Significantly higher levels of deoxyinosine and inosine are detected in nuclear DNA and RNA prepared from Itpa-deficient embryos compared to wild type embryos. Accumulation of ITP and dITP is responsible for the harmful effects observed in the Itpa-deficient mouse
malfunction
-
enzyme knockdown sensitizes HeLa cells to 6-N-hydroxylaminopurine-induced DNA breaks and apoptosis, and results in elevated mutagenesis in response to 6-N-hydroxylaminopurine treatment. Individuals with defective ITPase are predisposed to genome damage by impurities in nucleotide pools. They are also at an elevated risk for degenerative diseases and cancer
physiological function
-
the enzyme prevents 6-N hydroxylaminopurine-induced apoptosis, DNA damage and mutagenesis in human cells
physiological function
-
extracellular ATP, by upregulating ecto-nucleoside triphosphate diphosphohydrolase 2 and ecto-5'-nucleotidase and altering the enzyme membrane topology, affects local kinetics of ATP metabolism and signal transduction
physiological function
-
parasites with high enzymic activity show increased survival rate in LPS/IFN-gamma-activated mouse cells, by inhibiting the host-cell NO production. Inhibition of enzyme activity reduces the parasite survival rates, an effect associated with increased macrophage NO production. Enzymic activity generates substrate for the production of extracellular adenosine, which binds to A2B receptors and reduces IL-12 and TNF-alpha produced by activated macrophages, thus inhibiting NO production
physiological function
-
upon combined expression of human ecto-5'-nucleotidase and ecto-nucleoside triphosphate diphosphohydrolase 1 in pig endothelial cells using F2A sequence bearing construct, addition of AMP increases production of adenosine in the medium to 14.2 microM while it remains below 1 microM in controls. A marked increase of adenosine formation from ADP or ATP is observed only in cells transfected with both enzymes
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