3.6.1.23 dCTP + H2O - 3.6.1.23 dUTP + H2O - 3.6.1.23 dUTP + H2O removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA 3.6.1.23 dUTP + H2O removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, essential for replication and cell survival 3.6.1.23 dUTP + H2O removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, provides substrate for dTTP synthesis 3.6.1.23 dUTP + H2O removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, provides the substrate thymidylate synthase and is therefore essential for the synthesis of dTTP 3.6.1.23 dUTP + H2O biological roles and functions of dUTPase-related proteins and domains, overview 3.6.1.23 dUTP + H2O dUMP is required for biosynthesis of dTTP, overview 3.6.1.23 dUTP + H2O the enzyme is essential in the lytic cycle of the virus 3.6.1.23 dUTP + H2O the enzyme prevents incorporation of uracil into DNA by strict regulation of the cellular dUTP to dTTP ratio, developmental regulation of the isozymes at mRNA and protein levels 3.6.1.23 dUTP + H2O the enzyme regulates the levels of dUTP 3.6.1.23 dUTP + H2O the essential enzyme is responsible for preventive DNA repair via exclusion of uracil, overview, lack of negative enzyme regulation leads to thymine-less cell death in cells performing active DNA synthesis 3.6.1.23 dUTP + H2O the reaction produces the primary source of substrate for synthesis of dTTP and reduces the intracellular dUTP concentration, thus limiting the misincorporation of uracil into DNA 3.6.1.23 dUTP + H2O a preventive DNA repair enzyme, contributes to maintain the appropriate cellular dUTP/dTTP ratio by catalyzing dUTP hydrolysis, dUTPase is essential for viability 3.6.1.23 dUTP + H2O dUTPase is essential for DNA integrity and is an important survival factor for cancer cells 3.6.1.23 dUTP + H2O dUTPase is essential in controlling relative cellular levels of dTTP/dUTP, both of which can be incorporated into DNA 3.6.1.23 dUTP + H2O dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis 3.6.1.23 dUTP + H2O enzyme inhibition is involved in apoptosis in cancer cells and decreases the sensitivity of cells for 5-fluorouracil, overview 3.6.1.23 dUTP + H2O the enzyme is one of the primary enzymes that prevent the incorporation and accumulation of deoxyuridine in genomic DNA, and is essential for viability 3.6.1.23 dUTP + H2O the enzyme is responsible for maintaining a low dUTP level in order to avoid the incorporation of uracil into DNA, and for providing dUMP as a substrate for deoxythymidine triphosphate biosynthesis 3.6.1.23 dUTP + H2O the enzyme plays an essential role in nucleotide biosynthesis, dUMP is required for de novo synthesis of dTTP. The enzyme maintains low cellular ratios of dUTP:dTTP, thus preventing the misincorporation of uracil into chromosomal DNA 3.6.1.23 dUTP + H2O an efficient preventive repair pathway, avoiding uracil in DNA, is generally present that keeps cellular dUTP/dTTP levels at a much decreased value to prevent use of dUTP as a building block by DNA polymerases. The enzyme responsible for this sanitizing role is dUTPase, a ubiquitous protein 3.6.1.23 dUTP + H2O dUTP is constantly produced in the pyrimidine biosynthesis network. To prevent uracil incorporation into DNA, representatives of the dUTP nucleotidohydrolase enzyme family eliminate excess dUTP as one moethod to avoid uracil nucleotides incorporation into DNA, besides exchanging dUTP for dTTP as a second method, overview 3.6.1.23 dUTP + H2O dUTPase catalyzes the hydrolysis of dUTP to dUMP and diphosphate controlling the incorporation of uracil into DNA genomes 3.6.1.23 dUTP + H2O dUTPase has a dual role in pyrimidine nucleotide metabolism, it provides the substrate for the thymidylate synthase allowing the formation of dTTP. Secondly, the enzyme is responsible for keeping dUTP intracellular levels low, avoiding its misincorporation into nascent DNA 3.6.1.23 dUTP + H2O the enzyme has two major roles in maintaining the correct free nucleotide balance in the cell. It provides dUMP, a major cellular source for dTMP which is in turn needed for dTTP formation. It also maintains the concentration of dUTP lower than that of dTTP thereby minimizing mistaken incorporation of dUTP into DNA 3.6.1.23 dUTP + H2O enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP 3.6.1.23 dUTP + H2O the enzyme is important in preventing dUTP from being incorporated into DNA and may have a significant role in both the synthesis of thymidine- and diphosphate-dependent phosphorylation 3.6.1.23 dUTP + H2O the enzyme prevents a deleterious incorporation of uracil into DNA 3.6.1.23 dUTP + H2O elimination of dUTP, by dUTPase, is vital since its misincorporation into DNA by DNA polymerases can initiate a damaging iterative repair and misincorporation cycle, resulting in DNA fragmentation and cell death, the anti-tumour activity of folate agonists and thymidylate synthase inhibitors is thought to rely on UTP misincorporation. dUTPase activity is an ideal point of intervention in both chemotherapy and anti-retroviral therapy 3.6.1.23 dUTP + H2O the enzyme may generally perform an essential role in DNA replication and therefore can serve as a target enzyme for the development of chemotherapeutic compounds 3.6.1.23 dUTP + H2O enzyme plays a key role in deoxyribonucleotide metabolism 3.6.1.23 dUTP + H2O enzyme is important in DNA replication 3.6.1.23 dUTP + H2O enzyme is involved in controlling intracellular dUTP levels 3.6.1.23 dUTP + H2O enzyme of pyrimidine deoxyribonucleotide metabolism 3.6.1.23 dUTP + H2O lethality of a mutation in the dut gen, deoxyuridine triphosphatase. The dut gene product might have an essential function apart from its deoxyuridine triphosphatase activity 3.6.1.23 additional information biological functions in housekeeping, overview 3.6.1.23 additional information overexpression of dUTPase is associated with resistance to chemotherapeutic agents targeting thymidilate biosynthesis 3.6.1.23 additional information the enzyme is essential for survival 3.6.1.23 additional information procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation 3.6.1.23 additional information the enzyme has immunomodulatory function in pathogenesis, treatment of human monocyte-derived macrophages with dUTPase from Ebstein-Barr virus induces the expression of proinflammatory cytokines, e.g. interleukin-6, through activation of NF-kappaB via TLR2 receptor, but not TLR3 or TLR4, requiring the adaptor molecule MyD88, but not CD14, overview 3.6.1.23 additional information the enzyme limits the activation or degradation of 5-fluorouracil, overview. The expression of dUTPase is significantly different between primary tumours and their corresponding metastatic tumour