Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2',3'-dideoxyUTP + H2O
2',3'-dideoxy-UMP + diphosphate
-
76% of the activity with dUTP
-
-
?
2'-deoxy-5-fluoro-UTP + H2O
2'-deoxy-5-fluoro-UMP + diphosphate
6-azaUTP + H2O
6-azaUMP + diphosphate
-
39% of the activity with dUTP
-
-
?
alpha,beta-imido-dUTP + H2O
dUMP + amino-diphosphate
O92810
-
-
-
?
araUTP + H2O
araUMP + diphosphate
-
90% of the activity with dUTP
-
-
?
beta-L-2'-dUTP + H2O
beta-L-2'-dUMP + diphosphate
dATP + H2O
dAMP + diphosphate
dCTP + H2O
dCMP + diphosphate
dGTP + H2O
dGMP + diphosphate
dITP + H2O
dIMP + diphosphate
shows also significant activity against dITP
-
-
?
dTTP + H2O
dTMP + diphosphate
dUDP + H2O
deoxyuridine + diphosphate
dUDP + H2O
dUMP + phosphate
dUTP + H2O
dUMP + diphosphate
dUTP-Co2+ + H2O
dUMP-Co2+ + diphosphate
-
-
-
-
?
dUTP-Mg2+ + H2O
dUMP-Mg2+ + diphosphate
-
-
-
-
?
dUTP-Mn2+ + H2O
dUMP-Mn2+ + diphosphate
-
-
-
-
?
dUTPalphaS + H2O
dUMP + thiodiphosphate
-
-
-
-
?
UTP + H2O
UMP + diphosphate
additional information
?
-
2'-deoxy-5-fluoro-UTP + H2O
2'-deoxy-5-fluoro-UMP + diphosphate
-
most specific substrate
-
-
?
2'-deoxy-5-fluoro-UTP + H2O
2'-deoxy-5-fluoro-UMP + diphosphate
-
most specific substrate
-
-
?
beta-L-2'-dUTP + H2O
beta-L-2'-dUMP + diphosphate
-
-
-
-
?
beta-L-2'-dUTP + H2O
beta-L-2'-dUMP + diphosphate
-
-
-
-
?
dATP + H2O
dAMP + diphosphate
-
-
-
-
?
dATP + H2O
dAMP + diphosphate
-
-
-
-
?
dATP + H2O
dAMP + diphosphate
-
low activity
-
-
?
dATP + H2O
dAMP + diphosphate
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
-
no activity
-
-
?
dCTP + H2O
dCMP + diphosphate
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
-
low activity
-
-
?
dCTP + H2O
dCMP + diphosphate
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
-
-
-
?
dCTP + H2O
dCMP + diphosphate
about 10fold lower activity with dCTP compared to dUTP
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
-
?
dGTP + H2O
dGMP + diphosphate
-
low activity
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
no activity
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
low activity
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
-
-
-
-
?
dUDP + H2O
deoxyuridine + diphosphate
-
the enzyme is highly specific for deoxyuridine nucleotides
-
-
?
dUDP + H2O
deoxyuridine + diphosphate
-
-
-
-
?
dUDP + H2O
deoxyuridine + diphosphate
-
the enzyme is highly specific for deoxyuridine nucleotides
-
-
?
dUDP + H2O
dUMP + phosphate
-
-
-
-
?
dUDP + H2O
dUMP + phosphate
-
-
-
-
?
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
-
-
?
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
-
-
?
dUTP + H2O
?
-
enzyme plays a key role in deoxyribonucleotide metabolism
-
-
?
dUTP + H2O
?
-
the enzyme prevents a deleterious incorporation of uracil into DNA
-
-
?
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
-
-
?
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
-
-
?
dUTP + H2O
?
enzyme is important in DNA replication
-
-
?
dUTP + H2O
?
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
?
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
-
-
?
dUTP + H2O
?
-
enzyme is involved in controlling intracellular dUTP levels
-
-
?
dUTP + H2O
?
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
?
dUTP + H2O
?
-
enzyme of pyrimidine deoxyribonucleotide metabolism
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
dUTPase catalyzes the hydrolysis of dUTP to dUMP and diphosphate controlling the incorporation of uracil into DNA genomes
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for deoxyuridine nucleotides
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, provides substrate for dTTP synthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
highest activity
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
a preventive DNA repair enzyme, contributes to maintain the appropriate cellular dUTP/dTTP ratio by catalyzing dUTP hydrolysis, dUTPase is essential for viability
-
-
?
dUTP + H2O
dUMP + diphosphate
substrate binding structure, the strictly conserved residue Ser72 is involved in phosphate chain binding, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
biological roles and functions of dUTPase-related proteins and domains, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
most specific substrate
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential for DNA integrity and is an important survival factor for cancer cells
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential in controlling relative cellular levels of dTTP/dUTP, both of which can be incorporated into DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
enzyme inhibition is involved in apoptosis in cancer cells and decreases the sensitivity of cells for 5-fluorouracil, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is one of the primary enzymes that prevent the incorporation and accumulation of deoxyuridine in genomic DNA, and is essential for viability
-
-
?
dUTP + H2O
dUMP + diphosphate
substrate synthesis, overview, the enzymatic cycle is limited by a single rate-limiting step that occurs before or is concomitant with proton release
-
-
?
dUTP + H2O
dUMP + diphosphate
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
dUMP is required for de novo biosynthesis of thymine
-
?
dUTP + H2O
dUMP + diphosphate
-
dUTPase catalyzes the hydrolysis of dUTP to dUMP and diphosphate controlling the incorporation of uracil into DNA genomes
-
-
?
dUTP + H2O
dUMP + diphosphate
catalysis proceeds by way of an SN2 mechanism, a water molecule initiates in-line nucleophilic attack, conformational changes during the reaction take place in the C-terminus. The dUTPase binding pocket is highly specific for uracil, structural basis, overview. Phosphate chain coordination involves Mg2+ and is analogous to that of DNA polymerases. Catalytically competent and noncompetent conformation of the bound substrate, nodelling, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for deoxyuridine nucleotides
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is essential in the lytic cycle of the virus
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, essential for replication and cell survival
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
O92810
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
development of a robust and continuous dUTPase enzyme activity assay method using phenolred indicator, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
development of a robust and continuous dUTPase enzyme activity assay method using phenolred indicator, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
dUMP is required for biosynthesis of dTTP, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
most specific substrate
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
dUTPase catalyzes the hydrolysis of the alpha,beta-diphosphate bond of dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme regulates the levels of dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
Spbetavirus SPbeta
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
preferred substrate
-
-
?
dUTP + H2O
dUMP + diphosphate
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
substrate binding structure analysis, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
UTP + H2O
UMP + diphosphate
-
-
-
-
?
UTP + H2O
UMP + diphosphate
-
-
-
-
?
UTP + H2O
UMP + diphosphate
-
-
-
-
?
UTP + H2O
UMP + diphosphate
-
-
-
-
?
UTP + H2O
UMP + diphosphate
-
-
-
-
?
UTP + H2O
UMP + diphosphate
-
at about 3% of the activity with dUTP
-
-
?
UTP + H2O
UMP + diphosphate
substrate for mutant enzyme Y88A
-
-
?
additional information
?
-
the enzyme does not hydrolyze dATP, dTTP, dCTP, or dGTP
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze dATP, dTTP, dCTP, or dGTP
-
-
-
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
-
no hydrolysis of dUDP
-
-
?
additional information
?
-
-
comparison of the Drosophila melanogaster and the Escherichia coli enzymes
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
comparison of the Drosophila melanogaster and the Escherichia coli enzymes
-
-
?
additional information
?
-
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
-
no activity with dUMP
-
-
-
additional information
?
-
-
overexpression of dUTPase is associated with resistance to chemotherapeutic agents targeting thymidilate biosynthesis
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
-
the enzyme binds non-cooperatively to 2'-dUMP
-
-
?
additional information
?
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
the bifunctional dCTP deaminase:dUTPase shows very similar affinities for dCTP and deoxyuridine triphosphate as substrates, overview
-
-
?
additional information
?
-
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
?
additional information
?
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
?
additional information
?
-
the bifunctional dCTP deaminase:dUTPase shows very similar affinities for dCTP and deoxyuridine triphosphate as substrates, overview
-
-
?
additional information
?
-
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
?
additional information
?
-
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
alpha,beta-imido dUTP is a non-hydrolysable substrate
-
-
?
additional information
?
-
-
alpha,beta-imido dUTP is a non-hydrolysable substrate
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
the enzyme is essential for survival
-
-
?
additional information
?
-
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
?
additional information
?
-
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
?
additional information
?
-
no activity with dUMP
-
-
-
additional information
?
-
-
no activity with dUMP
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dCTP + H2O
dCMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
additional information
?
-
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
-
-
?
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
-
-
?
dUTP + H2O
?
-
enzyme plays a key role in deoxyribonucleotide metabolism
-
-
?
dUTP + H2O
?
-
the enzyme prevents a deleterious incorporation of uracil into DNA
-
-
?
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
-
-
?
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
-
-
?
dUTP + H2O
?
enzyme is important in DNA replication
-
-
?
dUTP + H2O
?
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
?
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
-
-
?
dUTP + H2O
?
-
enzyme is involved in controlling intracellular dUTP levels
-
-
?
dUTP + H2O
?
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
?
dUTP + H2O
?
-
enzyme of pyrimidine deoxyribonucleotide metabolism
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
dUTPase catalyzes the hydrolysis of dUTP to dUMP and diphosphate controlling the incorporation of uracil into DNA genomes
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, provides substrate for dTTP synthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
a preventive DNA repair enzyme, contributes to maintain the appropriate cellular dUTP/dTTP ratio by catalyzing dUTP hydrolysis, dUTPase is essential for viability
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
biological roles and functions of dUTPase-related proteins and domains, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential for DNA integrity and is an important survival factor for cancer cells
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential in controlling relative cellular levels of dTTP/dUTP, both of which can be incorporated into DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
enzyme inhibition is involved in apoptosis in cancer cells and decreases the sensitivity of cells for 5-fluorouracil, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is one of the primary enzymes that prevent the incorporation and accumulation of deoxyuridine in genomic DNA, and is essential for viability
-
-
?
dUTP + H2O
dUMP + diphosphate
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
dUMP is required for de novo biosynthesis of thymine
-
?
dUTP + H2O
dUMP + diphosphate
-
dUTPase catalyzes the hydrolysis of dUTP to dUMP and diphosphate controlling the incorporation of uracil into DNA genomes
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme is essential in the lytic cycle of the virus
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA, essential for replication and cell survival
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
dUMP is required for biosynthesis of dTTP, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
the enzyme regulates the levels of dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
Spbetavirus SPbeta
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
-
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
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
-
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
overexpression of dUTPase is associated with resistance to chemotherapeutic agents targeting thymidilate biosynthesis
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
additional information
?
-
the enzyme is essential for survival
-
-
?
additional information
?
-
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
?
additional information
?
-
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
?
additional information
?
-
-
biological functions in housekeeping, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(E)-3-(2,2-difluoroethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(E)-3-(cyclopentyloxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(E)-3-(cyclopropylmethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)-3-methoxybenzenesulfonamide
-
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
(R)-1-(3-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-ylsulfonyl)propyl)pyrimidine-2,4(1H,3H)-dione
-
(R)-1-(4-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-yl)-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
(R)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
-
(R)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
-
(R)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-benzenesulfonamide
-
(R,E)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
-
(R,E)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
-
(R,E)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
-
(S)-1-(4-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-yl)-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(2-amido-4-trityloxybutyl)uracil
-
1-(2-dimethylamido-4-trityloxybutyl)uracil
-
1-(2-morpholinamido-4-trityloxybutyl)uracil
-
1-(3-tert-butyldimethylsilyloxypropyl)uracil
1-(3-triphenylsilyloxypropyl)uracil
1-(3-tritylaminopropyl)uracil
1-(3-trityloxypropyl)uracil
1-(3-[[(2S)-2-[hydroxy[bis(2-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
-
1-(3-[[(2S)-2-[hydroxy[bis(3-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(3-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(4-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(4-[(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
1-(5-triphenylsilyloxypentyl)uracil
1-(5-tritylaminopentyl)uracil
1-(5-trityloxypentyl)uracil
1-[(1E,8E)-5-([[(E)-(3,4-dihydroxy-5-methoxybenzylidene)amino]oxy]methyl)-1-(3,4-dihydroxy-5-methoxyphenyl)-3,7-dioxa-2,8-diazadeca-1,8-dien-10-yl]pyrimidine-2,4(1H,3H)-dione
-
1-[(1Z,8E)-5-([[(E)-(3,4-dihydroxy-5-methoxybenzylidene)amino]oxy]methyl)-1-(3,4-dihydroxy-5-methoxyphenyl)-3,7-dioxa-2,8-diazadeca-1,8-dien-10-yl]pyrimidine-2,4(1H,3H)-dione
-
1-[(2E)-4-(trityloxy)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
1-[(2R,5S)-5-([[tert-butyl(diphenyl)silyl]oxy]methyl)-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
-
1-[(2R,5S)-5-[(trityloxy)methyl]-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
-
1-[(E)-4-trityloxy-2-butenyl]uracil
1-[(Z)-4-trityloxy-2-butenyl]uracil
1-[2-(acetamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
-
1-[2-(acetamido)-4-(triphenylmethyl)aminobutyl]uracil
-
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
1-[2-(carbobenzoxymethyl)-4-(triphenylmethyl)aminobutyl]uracil
-
1-[2-(carboethoxyethylamido)-4-trityloxybutyl]uracil
-
1-[2-(carboxy)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
-
1-[2-(carboxy)-4-(triphenylmethyl)aminobutyl]uracil
-
1-[2-(carboxyethylamido)-4-trityloxybutyl]uracil
-
1-[2-(diethylamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
-
1-[2-(ethylamido)-4-(tert-butyldiphenylsilyloxy) butyl]uracil
-
1-[2-(hydroxyethylamido)-4-trityloxybutyl]uracil
-
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
1-[2-(methoxyethylamido)-4-trityloxybutyl]uracil
-
1-[2-(methylamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
-
1-[2-(N,N-dimethylaminoethylamido)-4-trityloxybutyl]uracil
-
1-[2-(N-benzyloxycarbonylpiperazinamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
-
1-[2-(N-methylpiperazine)amido-4-trityloxybutyl]uracil
-
1-[2-(tert-butyldiphenylsilyloxyethylamido)-4-trityloxybutyl]uracil
-
1-[2-(trityloxy)ethoxymethyl]uracil
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-(benzhydrylaminocarbonyl)propyl]uracil
-
1429fold selectivity over human enzyme
1-[3-(tritylamino)propyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-(tritylaminocarbonyl)propyl]uracil
-
4545fold selectivity over human enzyme
1-[3-([(2R)-2-[hydroxy(diphenyl)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-([(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-([(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
1-[3-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
1-[4-hydroxy-3-[(tritylamino)methyl]butyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[bis[2-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[bis[3-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[bis[4-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[4-[(2S)-2-[hydroxy[di(thiophen-3-yl)]methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
1-[6-(tritylamino)hexyl]pyrimidine-2,4(1H,3H)-dione
-
1-[N-(2-triphenylmethylaminoethyl)-acetamide]uracil
-
-
1-[N-(3-triphenylmethylaminopropyl)-acetamide]uracil
-
-
1-[N-(4-triphenylmethylaminobutyl)-acetamide]uracil
-
-
1-[N-(triphenylmethyl) diaminodi(n-propyl) acetamide]uracil
-
-
1-[N-(triphenylmethylaminoethyl)-N-(aminoethyl) acetamide]uracil
-
-
1-[N-hydroxyethyl-N-(triphenylmethylamino) ethyl-acetamide]uracil
-
-
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
2',3',5'-trideoxy-3'-fluoro-5'-(tritylamino)uridine
-
activity against the parasites with IC50: 0.0053 mM
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
2',5'-dideoxy-5'-(tritylamino)uridine
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
2'-deoxy-5'-O-(triphenylsilyl)uridine
-
activity against the parasites with IC50: 0.0011 mM
2'-deoxy-5'-O-trityluridine
2'-deoxy-5'-O-[tris(1-methylethoxy)silyl]uridine
-
activity against the parasites with IC50: 0.013 mM
2'-deoxy-5'-phenylmethylaminouracil
-
-
2'-deoxy-5'-triphenylmethanyluracil
-
-
2'-deoxyuracil 5'-diphenyl phosphate
-
-
2'-deoxyuridine
-
competitive inhibition
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
3'-azido-2',3'-dideoxy-UTP
-
competitive inhibitor
3'-deoxy-5'-O-(hydroxy{[hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl)uridine
3'-deoxy-5'-O-[hydroxy(phosphonoamino)phosphoryl]uridine
competitive inhibition
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
3-(2,2-difluoroethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methylbutan-2-yl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylethyl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylhexan-3-yl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-phenylpropyl)propanamide
-
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)propanamide
-
3-(cyclopentyloxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
3-(cyclopropylmethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
3-(cyclopropylmethoxy)-N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
-
3-[5-(trityloxy)tetrahydrofuran-2-yl]pyridine-2,6(1H,3H)-dione
-
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methyl-1,1-diphenylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)-N-methylbutanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-hydroxy-2,2-diphenylethyl)-N-methylbutanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-1-phenylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-4-phenylbutan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylpropan-2-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylpentan-3-yl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)butanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-phenylbutanamide
-
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-[2-methyl-1-(naphthalen-2-yl)propan-2-yl]butanamide
-
4-hydroxymercuribenzoate
-
5 mM, complete inhibition
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2',3'-dideoxyuracil
-
-
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2'-deoxyuracil
-
-
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-3'-methyl-2',3'-dideoxyuracil
-
-
5'-(2,3,3-trimethylbutan-2-yl)-3'-methyl-2',3'-dideoxyuracil
-
-
5'-(2,4-dimethyl-3-(1-methylethyl)pentan-3-yl)-2'-deoxyuracil
-
-
5'-(P3-benzyl-alpha,beta-methylene)-2'deoxyuridine
-
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
-
5'-hexadecanoyl-3'-methyl-2',3'-dideoxyuracil
-
-
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
5'-O-(4,4'-dimethoxytrityl)-2'-deoxyuridine
-
-
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
5'-O-triphenylsilyl-2'-deoxyuridine
5'-pentanoylamino-2',5'-dideoxyuridine
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
5'-tritylamino-2',5'-dideoxyuridine
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
5-Aminouracil
-
5 mM, 50% loss of activity
6-aminouracil
-
5 mM, 60% loss of activity
8-azido-ATP
-
competitive
alpha-beta-imido-dUTP
-
competitive, strong inhibition
Ba2+
Spbetavirus SPbeta
-
-
bacteriophage PBS2-induced inhibitor
-
seems to form a high MW complex with the Bacillus subtilis dUTPase, the lower MW enzyme form of dUTPase is not inactivated by the protease inhibitor
-
beta-hydroxyisovalerylshikonin
an ATP-noncompetitive inhibitor of protein tyrosine kinases, induces apoptosis in human lung cancer DMS114 cells through reduction of dUTP nucleotidohydrolase activity, acts synergistically with 5-fluorouracil, overview
bovine serum albumin
38% inhibition at 0.01%
-
Cd2+
Spbetavirus SPbeta
-
-
guanidine hydrochloride
kinetics of GuHCl-induced denaturation of the two dUTPase isozymes at pH 7.5, 4 °C and 1.5-4 M
KCl
-
0.4 mM, 29% loss of activity
Mg2+
-
complete inhibition by extensive dialysis against 0.0125 M MgCl2
N,N-dibenzyl-3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)propanamide
-
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)-3-methoxybenzenesulfonamide
-
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)benzenesulfonamide
-
N-benzyl-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)butanamide
-
N-tert-butyl-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)butanamide
-
N-[(1R)-1-[3-(cyclopropylmethoxy)-4-fluorophenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
-
N-[(1R)-1-[3-(cyclopropylmethoxy)phenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-D-alanyl-L-tyrosine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-aspartic acid
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-glutamic acid
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-glutamine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-lysine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-threonine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanylglycine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-lysine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-threonine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-tyrosine
-
-
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycylglycine
-
-
N-[2-[3-(cyclopropylmethoxy)phenyl]propan-2-yl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
-
N-[3-(tert-butyl diphenyl silanyloxy)-propyl]-2-uracil acetamide
-
-
N-[4-(tert-butyl diphenyl silanyloxy)-butyl]-2-uracil acetamide
-
-
N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
-
NEM
-
12 mM, 14% loss of activity
siRNAdUT3
a 21 base-pair double-stranded RNA molecule targeted against the motif 3 of the enzyme, time- and dose-dependent decrease in the dUTPase activity in transfected cells
-
staphylococcal repressor protein StlSaPIBov1
-
highly potent inhibitor
-
Stl repressor protein from Staphylococcus aureus
-
-
-
thymidine 5'-(alpha,beta-imido)triphosphate
-
thymidine triphosphate
binding of thymidine triphosphate leads to disordered C-terminal arranged as a lid covering the active site, and the enzyme adapts an inactive conformation as a result of structural changes in the active site, mechanism, overview
1,10-phenanthroline
-
-
1,10-phenanthroline
-
50 mM, 30% inhibition
1-(3-tert-butyldimethylsilyloxypropyl)uracil
-
-
1-(3-tert-butyldimethylsilyloxypropyl)uracil
-
-
1-(3-triphenylsilyloxypropyl)uracil
-
-
1-(3-triphenylsilyloxypropyl)uracil
-
-
1-(3-tritylaminopropyl)uracil
-
-
1-(3-tritylaminopropyl)uracil
-
-
1-(3-trityloxypropyl)uracil
-
-
1-(3-trityloxypropyl)uracil
-
-
1-(5-triphenylsilyloxypentyl)uracil
-
-
1-(5-triphenylsilyloxypentyl)uracil
-
-
1-(5-tritylaminopentyl)uracil
-
-
1-(5-tritylaminopentyl)uracil
-
-
1-(5-trityloxypentyl)uracil
-
-
1-(5-trityloxypentyl)uracil
-
-
1-[(E)-4-trityloxy-2-butenyl]uracil
-
-
1-[(E)-4-trityloxy-2-butenyl]uracil
-
-
1-[(Z)-4-trityloxy-2-butenyl]uracil
-
-
1-[(Z)-4-trityloxy-2-butenyl]uracil
-
-
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
-
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
-
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
-
-
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
-
-
1-[2-(trityloxy)ethoxymethyl]uracil
-
-
1-[2-(trityloxy)ethoxymethyl]uracil
-
-
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
-
-
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
-
-
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
-
-
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
-
-
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
-
-
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
-
-
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
-
-
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
-
-
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
-
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
-
-
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
-
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
-
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
-
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
-
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
-
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
-
activity against the parasites with IC50: 0.0020 mM, binding structure involving Tyr112, Ile117, Ile108, and Asn103, overview
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
-
2',5'-dideoxy-5'-(tritylamino)uridine
-
activity against the parasites with IC50: 0.0045 mM
2',5'-dideoxy-5'-(tritylamino)uridine
-
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
2'-deoxy-5'-O-trityluridine
-
2'-deoxy-5'-O-trityluridine
-
activity against the parasites with IC50: 0.006 mM
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
-
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
-
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
best inhibitor
3'-deoxy-5'-O-(hydroxy{[hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl)uridine
competitive inhibition
3'-deoxy-5'-O-(hydroxy{[hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl)uridine
-
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
-
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
-
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
-
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
-
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
5'-pentanoylamino-2',5'-dideoxyuridine
-
-
5'-pentanoylamino-2',5'-dideoxyuridine
-
-
5'-pentanoylamino-2',5'-dideoxyuridine
-
-
5'-pentanoylamino-2',5'-dideoxyuridine
-
-
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
5'-tritylamino-2',5'-dideoxyuridine
-
-
5'-tritylamino-2',5'-dideoxyuridine
-
-
5'-tritylamino-2',5'-dideoxyuridine
-
-
5'-tritylamino-2',5'-dideoxyuridine
-
-
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
-
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
-
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
-
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
-
alpha,beta-imido-dUDP
-
potent inhibition
alpha,beta-imido-dUDP
-
-
alpha,beta-imido-dUTP
substrate analogue, inhibits the wild-type enzyme, not mutant S72A
alpha,beta-imido-dUTP
-
-
alpha,beta-imido-dUTP
-
-
alpha,beta-imido-dUTP
-
competitive inhibition
Ca2+
-
-
Ca2+
-
5 mM, 69% inhibition
Ca2+
Spbetavirus SPbeta
-
-
Cu2+
-
0.5 mM, 50% inhibition
dTMP
-
-
dTTP
-
-
dTTP
competitive feedback inhibition
dUDP
-
-
dUDP
-
competitive inhibition
dUMP
-
product inhibition
dUMP
-
product inhibition
dUMP
-
product, competitive inhibition
dUMP
-
product inhibition
dUTP
-
substrate inhibition at higher concentrations
EDTA
-
reversed by Mg2+, Mn2+, Zn2+, Co2+ and Ca2+
EDTA
-
1 mM, 65% loss of activity
EDTA
-
2 mM, complete inhibition
EDTA
-
reversed by Mg2+ or Zn2+
EDTA
-
0.5 mM, more than 90% inhibition
EDTA
-
dissociation of the enzyme into its monomeric form
EDTA
-
reversed by Mg2+, Co2+ or Mn2+
EDTA
-
reversed by Co2+ or Mg2+
EDTA
-
causes a 105fold decrease and a 12fold increase of the kcat and Km values for dUTP hydrolysis, respectively, compared to the dUTP-Mg2+ complex
EDTA
-
1 mM, 91% inhibition
EDTA
less than 10% residual activity at 1 mM
EDTA
-
reversed by Mg2+, Mn2+ or Zn2+
EGTA
-
-
EGTA
-
10 mM, more than 90% inhibition
fluorodeoxy-UMP
-
-
Hg2+
-
10 mM HgCl2, 50% inhibition in absence of mercaptoethanol
Mn2+
-
-
Mn2+
-
5 mM, 26% inhibition
Stl protein
-
-
-
Uracil
-
5 mM, 30% loss of activity
Zn2+
-
-
Zn2+
-
5 mM, 23% inhibition
additional information
-
several dUMP analogues with substituents at the 3'- or 5'-positions show poor inhibitory activity
-
additional information
-
the enzyme possesses a specific tryptic cleavage site Arg132-Ile133 20 A far from the active site of the enzyme, the enzyme is protected against tryptic digestion by binding alpha,beta-imino-dUTP which induces an allosteric conformational change within the central threefold channel of the homotrimer
-
additional information
-
the enzyme is not inhibited by 3'-azido-2',3'-dideoxy-UTP
-
additional information
-
binding of alpha,beta-imino-dUTP does not induce allosteric conformational changes and does not protect the enzyme against tryptic digestion
-
additional information
the wild type enzyme is not inhibited by staphylococcal repressor StlSaPIbov1 protein
-
additional information
-
the wild type enzyme is not inhibited by staphylococcal repressor StlSaPIbov1 protein
-
additional information
-
inhibitor in vivo activity against the parasite, overview
-
additional information
-
programmed cell death protein 4 downregulates dUTPase in certain cell types, overview
-
additional information
-
enzyme inhibitor development by high-throughput screening of triskelion libraries, a uracil-aldehyde ligand is covalently tethered to one position of a trivalent alkyloxyamine linker via an oxime linkage, and then the vacant linker positions are derivatized with a library of aldehydes, screening of triskelion oximes for inhibitory potency, overview
-
additional information
-
the enzyme is not inhibited by 3'-azido-2',3'-dideoxy-UTP
-
additional information
-
inhibitor in vivo activity against the parasite, overview
-
additional information
-
diphosphate has no effect on activity
-
additional information
-
inhibitor in vivo activity against the parasite, overview
-
additional information
fast screening for binding of potential inhibitors to the active site
-
additional information
-
fast screening for binding of potential inhibitors to the active site
-
additional information
-
no inhibition by dTTp, dGTP, dATP, and dCTP
-
additional information
-
inhibitor in vivo activity against the parasite, overview
-
additional information
-
growth inhibition potency in vitro, overview, molecular docking modeling study
-
additional information
-
design and synthesis of tert-butyl diphenyl silyl uracil acetamides inhibitors, molecular modelling, overview
-
additional information
-
computational docking of small molecules structures to the enzyme for inhibitor development, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00173 - 0.0061
2'-deoxy-5-fluoro-UTP
0.438 - 0.523
beta-L-2'-dUTP
0.0447
dITP
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
0.0027
dUTP-Co2+
-
pH 7.0, 25°C, recombinant enzyme
0.0019
dUTP-Mg2+
-
pH 7.0, 25°C, recombinant enzyme
0.0137
dUTP-Mn2+
-
pH 7.0, 25°C, recombinant enzyme
additional information
additional information
-
0.00173
2'-deoxy-5-fluoro-UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0061
2'-deoxy-5-fluoro-UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.438
beta-L-2'-dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.523
beta-L-2'-dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0094
dATP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
1.13
dATP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.077
dCTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.465
dCTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.687
dCTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.21
dGTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
1.96
dGTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.11
dTTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.29
dTTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.761
dTTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0062
dUDP
-
25°C
0.0001
dUTP
-
-
0.00017
dUTP
-
pH and temperature not specified in the publication
0.00022
dUTP
-
pH and temperature not specified in the publication
0.0004
dUTP
-
pH 7.5, 25°C
0.0004
dUTP
at pH 7.6 and 25°C
0.0006
dUTP
Spbetavirus SPbeta
-
pH 7.5, 25°C, recombinant enzyme
0.0006
dUTP
mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.00066
dUTP
-
pH 8.0, 25°C, recombinant enzyme
0.0007
dUTP
-
pH 7.6, 25°C, recombinant enzyme, in presence of 1 mM MgCl2
0.00071
dUTP
wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.0008
dUTP
wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.0009
dUTP
wild type enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C
0.00093
dUTP
-
wild type enzyme, at pH 7.5 and 20°C
0.00096
dUTP
-
pH and temperature not specified in the publication
0.001
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
0.0011
dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0011
dUTP
DELTA-loop mutant enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C
0.0011
dUTP
mutant enzyme R140K/H145W, at pH 7.5 and 20°C
0.0012
dUTP
-
recombinant enzyme
0.0013
dUTP
mutant enzyme H145W, at pH 7.5 and 20°C
0.0014
dUTP
wild type enzyme, at pH 7.5 and 20°C
0.0015
dUTP
-
in presence of Mg2+, at low concentrations of dUTP
0.0016
dUTP
wild type enzyme, at pH 8.0 and 25°C
0.0017
dUTP
mutant enzyme I117A, at pH 8.0 and 25°C
0.0017
dUTP
wild type enzyme, at pH 7.5 and 20°C
0.00179
dUTP
-
pH 7.4, 37°C, recombinant enzyme
0.0018
dUTP
at pH 7.5 and 20°C
0.0018
dUTP
mutant enzyme F46A, at pH 8.0 and 25°C
0.00187
dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0019
dUTP
-
pH 7.0, 25°C, recombinant enzyme
0.0019
dUTP
mutant enzyme K96A, at pH 8.0 and 25°C
0.002
dUTP
mutant enzyme V160D, at pH 7.5 and 20°C
0.0021
dUTP
mutant enzyme D170G, at pH 7.5 and 20°C
0.0024
dUTP
-
pH 5.7-6.2, recombinant enzyme
0.0025
dUTP
enzyme form DUT-N and DUT-M
0.0025
dUTP
mutant enzyme K150A, at pH 7.5 and 20°C
0.0026
dUTP
mutant enzyme K150E, at pH 7.5 and 20°C
0.0026
dUTP
mutant enzyme R158A, at pH 7.5 and 20°C
0.0026
dUTP
mutant enzyme R158E, at pH 7.5 and 20°C
0.0028
dUTP
mutant enzyme DELTA170-171, at pH 7.5 and 20°C
0.0029
dUTP
mutant enzyme R24T, at pH 7.5 and 20°C
0.0032
dUTP
mutant enzyme R158W, at pH 7.5 and 20°C
0.0036
dUTP
pH 7.4, 20°C, recombinant wild-type enzyme
0.0036
dUTP
-
mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
0.0037
dUTP
-
in presence of 1 mM Mg2+
0.004
dUTP
-
enzyme from uninfected KB cells
0.004
dUTP
-
in absence of Mg2+, at low concentrations of dUTP
0.004
dUTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.0042
dUTP
mutant enzyme R24T/S115R/D170G, at pH 7.5 and 20°C
0.0045
dUTP
mutant enzyme S115R, at pH 7.5 and 20°C
0.0048
dUTP
-
enzyme from herpes simplex virus type 1 infected KB cells
0.005
dUTP
mutant enzyme F166Y, at pH 7.5 and 20°C
0.0052
dUTP
mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.0052
dUTP
-
mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
0.0052
dUTP
-
mutant enzyme R166S, at pH 7.5 and 20°C
0.0054
dUTP
mutant enzyme R161K, at pH 7.5 and 20°C
0.006
dUTP
wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.0067
dUTP
mutant enzyme R24T/S115R, at pH 7.5 and 20°C
0.0067
dUTP
mutant enzyme T138STOP, at pH 7.5 and 20°C
0.007
dUTP
mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.0071
dUTP
mutant enzyme D170L, at pH 7.5 and 20°C
0.0073
dUTP
-
in the presence of 5 mM Mn2+, at pH 8.2 and 25°C
0.008
dUTP
mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.0082
dUTP
mutant enzyme G143STOP, at pH 7.5 and 20°C
0.009
dUTP
mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.0117
dUTP
-
pH 8.5, 50°C, recombinant enzyme
0.013
dUTP
mutant enzyme D34N, at pH 7.5 and 20°C
0.013
dUTP
-
mutant enzyme T22R/R116S, at pH 7.5 and 20°C
0.0132
dUTP
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
0.0142
dUTP
mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
0.021
dUTP
mutant enzyme DELTA134-153, at pH 7.5 and 20°C
0.0315
dUTP
mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
0.041
dUTP
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
0.45
dUTP
D90N mutant enzyme, pH 7.8, room temperature
0.5
dUTP
wild-type enzyme, pH 7.8, room temperature
3.788
dUTP
at pH 8.0 and 37°C
0.035
UTP
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
0.54
UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.571
UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
additional information
additional information
lower affinity for dUTP than strict dUTPases
-
additional information
additional information
-
lower affinity for dUTP than strict dUTPases
-
additional information
additional information
-
kinetics of dUTP binding
-
additional information
additional information
-
kinetics of dUTP binding
-
additional information
additional information
-
non-cooperative binding to 2'-dUMP, 1 molecule per enzyme subunit, kinetics and thermodynamics from isothermal titration microcalorimetry under different conditions, overview
-
additional information
additional information
detailed pre-steady-state and steady-state kinetic analysis, quantitative kinetic model of the human dUTPase catalytic cycle, overview
-
additional information
additional information
-
detailed pre-steady-state and steady-state kinetic analysis, quantitative kinetic model of the human dUTPase catalytic cycle, overview
-
additional information
additional information
ligand binding constants
-
additional information
additional information
-
ligand binding constants
-
additional information
additional information
steady-state kinetic analysis of the dual activities of the bifunctional enzyme, overview
-
additional information
additional information
-
Michaelis-Menten and ligand binding kinetics, overview. Thermodynamic parameters for the interaction between Plasmodium falciparum dUTPase and deoxyuridine derivatives at 25.2 °C and pH 7.0
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetics analysis
-
additional information
additional information
transient state kinetics of substrate binding to the S72A mutant dUTPase, stopped-flow measurements, overview. Comparative kinetics of formation of the enzyme-substrate complexes of the wild-type and S72A
-
additional information
additional information
-
transient state kinetics of substrate binding to the S72A mutant dUTPase, stopped-flow measurements, overview. Comparative kinetics of formation of the enzyme-substrate complexes of the wild-type and S72A
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.3
dITP
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
4.1
dUTP-Co2+
-
pH 7.0, 25°C, recombinant enzyme
13.3
dUTP-Mg2+
-
pH 7.0, 25°C, recombinant enzyme
5.3
dUTP-Mn2+
-
pH 7.0, 25°C, recombinant enzyme
5.3
UTP
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
1.5
dATP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.7
dCTP
-
pH 7.5, 25°C
1.6
dCTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
2.9
dGTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.1
dTTP
-
pH 7.5, 25°C
1.4
dTTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.0003
dUTP
D90N mutant enzyme, pH 7.8, room temperature
0.00089
dUTP
mutant enzyme G143STOP, at pH 7.5 and 20°C
0.0035
dUTP
mutant enzyme T138STOP, at pH 7.5 and 20°C
0.0045
dUTP
mutant enzyme R140K/H145W, at pH 7.5 and 20°C
0.007
dUTP
-
mutant enzyme D49N/F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
0.024
dUTP
mutant enzyme D28N/H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
0.04
dUTP
mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.04
dUTP
mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.053
dUTP
mutant enzyme R161K, at pH 7.5 and 20°C
0.06
dUTP
mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.18
dUTP
mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
0.32
dUTP
-
mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
0.45
dUTP
mutant enzyme R24T, at pH 7.5 and 20°C
0.51
dUTP
mutant enzyme R24T/S115R, at pH 7.5 and 20°C
0.53
dUTP
mutant enzyme D170L, at pH 7.5 and 20°C
0.67
dUTP
mutant enzyme DELTA134-153, at pH 7.5 and 20°C
0.7
dUTP
mutant enzyme H145W, at pH 7.5 and 20°C
0.88
dUTP
DELTA-loop mutant enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C
0.92
dUTP
mutant enzyme D34N, at pH 7.5 and 20°C
1.2
dUTP
mutant enzyme H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
1.2
dUTP
wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
1.2
dUTP
mutant enzyme F166Y, at pH 7.5 and 20°C
1.22
dUTP
wild type enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C
1.3
dUTP
mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
1.4
dUTP
wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
1.6
dUTP
wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
1.7
dUTP
mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
1.7
dUTP
mutant enzyme DELTA170-171, at pH 7.5 and 20°C
2.6
dUTP
mutant enzyme R158E, at pH 7.5 and 20°C
2.6
dUTP
mutant enzyme S115R, at pH 7.5 and 20°C
2.7
dUTP
-
mutant enzyme R166S, at pH 7.5 and 20°C
3
dUTP
wild type enzyme, at pH 7.5 and 20°C
3.1
dUTP
mutant enzyme R158W, at pH 7.5 and 20°C
3.1
dUTP
mutant enzyme R24T/S115R/D170G, at pH 7.5 and 20°C
3.2
dUTP
mutant enzyme R158A, at pH 7.5 and 20°C
3.3
dUTP
-
pH 7.6, 25°C, recombinant enzyme, in presence of 1 mM MgCl2
3.3
dUTP
mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
3.3
dUTP
-
mutant enzyme T22R/R116S, at pH 7.5 and 20°C
3.4
dUTP
-
pH 7.0, 25°C, recombinant enzyme
3.7 - 5.8
dUTP
pH 7.5, 25°C, recombinant wild-type and mutant enzymes
4.5
dUTP
-
pH 7.5, 25°C, in the absence of added metal ions
4.7
dUTP
at pH 7.5 and 20°C
5.5
dUTP
mutant enzyme K150E, at pH 7.5 and 20°C
5.8
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
5.9
dUTP
mutant enzyme K150A, at pH 7.5 and 20°C
6.2
dUTP
mutant enzyme D170G, at pH 7.5 and 20°C
6.3
dUTP
-
mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
6.58
dUTP
pH 7.4, 20°C, recombinant wild-type enzyme
6.8
dUTP
-
pH 8.5, 50°C, recombinant enzyme
6.8
dUTP
-
mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
7.4
dUTP
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
7.4
dUTP
wild type enzyme, at pH 7.5 and 20°C
7.4
dUTP
mutant enzyme V160D, at pH 7.5 and 20°C
8
dUTP
recombinant wild-type and mutant enzymes
9.3
dUTP
-
wild type enzyme, at pH 7.5 and 20°C
9.6
dUTP
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
9.7
dUTP
-
pH 7.4, 37°C, recombinant enzyme
11
dUTP
wild-type enzyme, pH 7.8, room temperature
11.33
dUTP
mutant enzyme F46A, at pH 8.0 and 25°C
11.67
dUTP
mutant enzyme K96A, at pH 8.0 and 25°C
11.67
dUTP
wild type enzyme, at pH 8.0 and 25°C
12
dUTP
mutant enzyme I117A, at pH 8.0 and 25°C
12.3
dUTP
-
pH 8.0, 25°C, recombinant enzyme
14.7
dUTP
-
pH 7.5, 25°C, in the presence of Mg2+ or Mn2+
18
dUTP
Spbetavirus SPbeta
-
pH 7.5, 25°C, recombinant enzyme
24.2
dUTP
-
pH 7.5, 25°C, in the presence of bis(acetylacetonato)oxovanadium(IV)
27.3
dUTP
-
pH 7.5, 25°C, in the presence of VO2+ or bis(acetylacetonato)oxovanadium(IV)
34
dUTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
48
dUTP
-
in the presence of 5 mM Mn2+, at pH 8.2 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
110 - 600
2'-deoxy-5-fluoro-UTP
0.00525 - 0.0061
beta-L-2'-dUTP
29
dITP
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
110
2'-deoxy-5-fluoro-UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
600
2'-deoxy-5-fluoro-UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.00525
beta-L-2'-dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0061
beta-L-2'-dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.00265
dATP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
16
dATP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.02172
dCTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.1616
dCTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
21
dCTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.00013
dGTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
14
dGTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
0.0092
dTTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.01971
dTTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
13
dTTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
6
dUTP
mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
8
dUTP
mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
8
dUTP
mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
9.8
dUTP
mutant enzyme R161K, at pH 7.5 and 20°C
20
dUTP
mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
32
dUTP
mutant enzyme DELTA134-153, at pH 7.5 and 20°C
62
dUTP
-
mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
71
dUTP
mutant enzyme D34N, at pH 7.5 and 20°C
74
dUTP
mutant enzyme R24T/S115R/D170G, at pH 7.5 and 20°C
75
dUTP
mutant enzyme D170L, at pH 7.5 and 20°C
76
dUTP
mutant enzyme R24T/S115R, at pH 7.5 and 20°C
90
dUTP
mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
100
dUTP
mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
160
dUTP
mutant enzyme R24T, at pH 7.5 and 20°C
180
dUTP
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
200
dUTP
wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
240
dUTP
mutant enzyme F166Y, at pH 7.5 and 20°C
250
dUTP
-
mutant enzyme T22R/R116S, at pH 7.5 and 20°C
520
dUTP
-
mutant enzyme R166S, at pH 7.5 and 20°C
580
dUTP
mutant enzyme S115R, at pH 7.5 and 20°C
610
dUTP
mutant enzyme DELTA170-171, at pH 7.5 and 20°C
740
dUTP
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
970
dUTP
mutant enzyme R158W, at pH 7.5 and 20°C
1000
dUTP
mutant enzyme R158E, at pH 7.5 and 20°C
1200
dUTP
mutant enzyme R158A, at pH 7.5 and 20°C
1800
dUTP
wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
1900
dUTP
-
mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
2100
dUTP
mutant enzyme K150E, at pH 7.5 and 20°C
2300
dUTP
wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
2400
dUTP
mutant enzyme K150A, at pH 7.5 and 20°C
2800
dUTP
mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C
3000
dUTP
mutant enzyme D170G, at pH 7.5 and 20°C
3700
dUTP
mutant enzyme V160D, at pH 7.5 and 20°C
4400
dUTP
wild type enzyme, at pH 7.5 and 20°C
5800
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C
6100
dUTP
mutant enzyme K96A, at pH 8.0 and 25°C
6300
dUTP
mutant enzyme F46A, at pH 8.0 and 25°C
6500
dUTP
-
in the presence of 5 mM Mn2+, at pH 8.2 and 25°C
6600
dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
7100
dUTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
7100
dUTP
mutant enzyme I117A, at pH 8.0 and 25°C
7300
dUTP
wild type enzyme, at pH 8.0 and 25°C
8500
dUTP
-
in the presence of 5 mM Mg2+, at pH 8.2 and 25°C
10000
dUTP
-
wild type enzyme, at pH 7.5 and 20°C
0.01121
UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.01278
UTP
-
at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
150
UTP
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0013
1-(2-amido-4-trityloxybutyl)uracil
pH and temperature not specified in the publication
0.0027
1-(2-dimethylamido-4-trityloxybutyl)uracil
pH and temperature not specified in the publication
0.0021
1-(2-morpholinamido-4-trityloxybutyl)uracil
pH and temperature not specified in the publication
0.073
1-(3-tert-butyldimethylsilyloxypropyl)uracil
0.0016 - 0.025
1-(3-triphenylsilyloxypropyl)uracil
0.0002 - 0.0014
1-(3-tritylaminopropyl)uracil
0.087 - 0.313
1-(3-trityloxypropyl)uracil
0.0038 - 1
1-(5-triphenylsilyloxypentyl)uracil
0.0043 - 1
1-(5-tritylaminopentyl)uracil
0.002 - 1
1-(5-trityloxypentyl)uracil
0.0033
1-[(1Z,8E)-5-([[(E)-(3,4-dihydroxy-5-methoxybenzylidene)amino]oxy]methyl)-1-(3,4-dihydroxy-5-methoxyphenyl)-3,7-dioxa-2,8-diazadeca-1,8-dien-10-yl]pyrimidine-2,4(1H,3H)-dione
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00009 - 0.006
1-[(2E)-4-(trityloxy)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
0.00021 - 0.017
1-[(2R,5S)-5-([[tert-butyl(diphenyl)silyl]oxy]methyl)-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
0.00039 - 0.0203
1-[(2R,5S)-5-[(trityloxy)methyl]-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
0.0006 - 1
1-[(E)-4-trityloxy-2-butenyl]uracil
0.0012 - 0.0052
1-[(Z)-4-trityloxy-2-butenyl]uracil
0.005
1-[2-(acetamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
pH and temperature not specified in the publication
0.0055
1-[2-(acetamido)-4-(triphenylmethyl)aminobutyl]uracil
pH and temperature not specified in the publication
0.023 - 1
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
0.0065
1-[2-(carbobenzoxymethyl)-4-(triphenylmethyl)aminobutyl]uracil
pH and temperature not specified in the publication
0.0005
1-[2-(carboethoxyethylamido)-4-trityloxybutyl]uracil
pH and temperature not specified in the publication
0.0016
1-[2-(carboxy)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
pH and temperature not specified in the publication
0.0072
1-[2-(carboxy)-4-(triphenylmethyl)aminobutyl]uracil
pH and temperature not specified in the publication
0.0002
1-[2-(carboxyethylamido)-4-trityloxybutyl]uracil
pH and temperature not specified in the publication
0.02
1-[2-(diethylamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
pH and temperature not specified in the publication
0.0057
1-[2-(ethylamido)-4-(tert-butyldiphenylsilyloxy) butyl]uracil
pH and temperature not specified in the publication
0.0004
1-[2-(hydroxyethylamido)-4-trityloxybutyl]uracil
pH and temperature not specified in the publication
0.0022 - 0.26
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
0.0014
1-[2-(methoxyethylamido)-4-trityloxybutyl]uracil
pH and temperature not specified in the publication
0.0036
1-[2-(methylamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
pH and temperature not specified in the publication
0.0078
1-[2-(N,N-dimethylaminoethylamido)-4-trityloxybutyl]uracil
pH and temperature not specified in the publication
0.098
1-[2-(N-benzyloxycarbonylpiperazinamido)-4-(tert-butyldiphenylsilyloxy)butyl]uracil
pH and temperature not specified in the publication
0.0056
1-[2-(N-methylpiperazine)amido-4-trityloxybutyl]uracil
pH and temperature not specified in the publication
0.01
1-[2-(tert-butyldiphenylsilyloxyethylamido)-4-trityloxybutyl]uracil
Ki above 0.01 mM, pH and temperature not specified in the publication
0.0007 - 0.017
1-[2-(trityloxy)ethoxymethyl]uracil
0.0007
1-[3-(benzhydrylaminocarbonyl)propyl]uracil
-
pH 8.0, temperature not specified in the publication
0.00004 - 0.028
1-[3-(tritylamino)propyl]pyrimidine-2,4(1H,3H)-dione
0.0002
1-[3-(tritylaminocarbonyl)propyl]uracil
-
pH 8.0, temperature not specified in the publication
0.0025 - 1
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
0.0013 - 0.074
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
0.0009 - 0.021
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
0.00024 - 0.0057
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
0.00004 - 0.029
1-[4-hydroxy-3-[(tritylamino)methyl]butyl]pyrimidine-2,4(1H,3H)-dione
0.00015 - 0.035
1-[6-(tritylamino)hexyl]pyrimidine-2,4(1H,3H)-dione
0.0373
1-[N-(2-triphenylmethylaminoethyl)-acetamide]uracil
-
-
0.0231
1-[N-(3-triphenylmethylaminopropyl)-acetamide]uracil
-
-
1
1-[N-(4-triphenylmethylaminobutyl)-acetamide]uracil
-
above
1
1-[N-(triphenylmethyl) diaminodi(n-propyl) acetamide]uracil
-
above
1
1-[N-(triphenylmethylaminoethyl)-N-(aminoethyl) acetamide]uracil
-
above
1
1-[N-hydroxyethyl-N-(triphenylmethylamino) ethyl-acetamide]uracil
-
above
0.0007 - 0.017
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
0.0125
2',3',5'-trideoxy-3'-fluoro-5'-(tritylamino)uridine
-
pH 5.7-6.2, recombinant enzyme
0.099 - 1
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
0.0048 - 0.406
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
0.00011 - 0.02
2',5'-dideoxy-5'-(tritylamino)uridine
0.026 - 1
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
0.0028
2'-deoxy-5'-O-(triphenylsilyl)uridine
-
pH 5.7-6.2, recombinant enzyme
0.0018
2'-deoxy-5'-O-trityluridine
-
pH 5.7-6.2, recombinant enzyme
0.2271
2'-deoxy-5'-O-[tris(1-methylethoxy)silyl]uridine
-
pH 5.7-6.2, recombinant enzyme
0.908
2'-deoxy-5'-triphenylmethanyluracil
-
pH 8.0, 25°C
0.135
2'-deoxyuracil 5'-diphenyl phosphate
-
pH 8.0, 25°C
0.018
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0093
3'-azido-2',3'-dideoxy-UTP
-
0.02 mM 3'-azido-2',3'-dideoxy-UTP in 0.05 mM bicine, with 5 mM MgCl2, pH and temperature not specified in the publication
0.067 - 1
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
0.088 - 1
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
0.156
3-[5-(trityloxy)tetrahydrofuran-2-yl]pyridine-2,6(1H,3H)-dione
-
pH 8.0, 25°C
0.805
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2'-deoxyuracil
-
pH 8.0, 25°C
0.807
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C
0.298 - 0.547
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
0.35
5'-hexadecanoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C
0.058 - 0.433
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
2.5
5'-O-(4,4'-dimethoxytrityl)-2'-deoxyuridine
-
25°C
0.082 - 1
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
0.0013 - 1
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
0.975 - 1
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
0.0028 - 1
5'-O-triphenylsilyl-2'-deoxyuridine
0.189 - 1
5'-pentanoylamino-2',5'-dideoxyuridine
0.089 - 1
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
0.0002 - 0.304
5'-tritylamino-2',5'-dideoxyuridine
0.012 - 1
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
0.00024
alpha,beta-imido-dUDP
-
25°C
0.0039
alpha,beta-imido-dUTP
pH 7.5, 25°C, wild-type enzyme
0.0009
alpha-beta-imido-dUTP
-
pH 8, 25°C
0.092
dUTP-Co2+
-
pH 7.0, 25°C, recombinant enzyme
0.0955
dUTP-Mg2+
-
pH 7.0, 25°C, recombinant enzyme
0.0718
dUTP-Mn2+
-
pH 7.0, 25°C, recombinant enzyme
0.000021
N-[(1R)-1-[3-(cyclopropylmethoxy)-4-fluorophenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
1
N-[3-(tert-butyl diphenyl silanyloxy)-propyl]-2-uracil acetamide
-
above
1
N-[4-(tert-butyl diphenyl silanyloxy)-butyl]-2-uracil acetamide
-
above
0.0000067
staphylococcal repressor protein StlSaPIBov1
-
at pH 7.5 and 20°C
-
additional information
2'-deoxy-5'-phenylmethylaminouracil
0.073
1-(3-tert-butyldimethylsilyloxypropyl)uracil
-
-
0.073
1-(3-tert-butyldimethylsilyloxypropyl)uracil
-
-
0.0016
1-(3-triphenylsilyloxypropyl)uracil
-
-
0.025
1-(3-triphenylsilyloxypropyl)uracil
-
-
0.0002
1-(3-tritylaminopropyl)uracil
-
-
0.0014
1-(3-tritylaminopropyl)uracil
-
-
0.087
1-(3-trityloxypropyl)uracil
-
-
0.313
1-(3-trityloxypropyl)uracil
-
-
0.0038
1-(5-triphenylsilyloxypentyl)uracil
-
-
1
1-(5-triphenylsilyloxypentyl)uracil
-
above
0.0043
1-(5-tritylaminopentyl)uracil
-
-
1
1-(5-tritylaminopentyl)uracil
-
above
0.002
1-(5-trityloxypentyl)uracil
-
-
1
1-(5-trityloxypentyl)uracil
-
above
0.00009
1-[(2E)-4-(trityloxy)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme K96A, at pH 8.0 and 25°
0.0006
1-[(2E)-4-(trityloxy)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
wild type enzyme, at pH 8.0 and 25°
0.0008
1-[(2E)-4-(trityloxy)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme I117A, at pH 8.0 and 25°
0.006
1-[(2E)-4-(trityloxy)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme F46A, at pH 8.0 and 25°
0.00021
1-[(2R,5S)-5-([[tert-butyl(diphenyl)silyl]oxy]methyl)-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme K96A, at pH 8.0 and 25°
0.0008
1-[(2R,5S)-5-([[tert-butyl(diphenyl)silyl]oxy]methyl)-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme I117A, at pH 8.0 and 25°
0.0012
1-[(2R,5S)-5-([[tert-butyl(diphenyl)silyl]oxy]methyl)-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
wild type enzyme, at pH 8.0 and 25°
0.017
1-[(2R,5S)-5-([[tert-butyl(diphenyl)silyl]oxy]methyl)-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme F46A, at pH 8.0 and 25°
0.00039
1-[(2R,5S)-5-[(trityloxy)methyl]-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme K96A, at pH 8.0 and 25°
0.0016
1-[(2R,5S)-5-[(trityloxy)methyl]-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme I117A, at pH 8.0 and 25°
0.0019
1-[(2R,5S)-5-[(trityloxy)methyl]-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
wild type enzyme, at pH 8.0 and 25°
0.0203
1-[(2R,5S)-5-[(trityloxy)methyl]-2,5-dihydrofuran-2-yl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme F46A, at pH 8.0 and 25°
0.0006
1-[(E)-4-trityloxy-2-butenyl]uracil
-
-
1
1-[(E)-4-trityloxy-2-butenyl]uracil
-
above
0.0012
1-[(Z)-4-trityloxy-2-butenyl]uracil
-
-
0.0052
1-[(Z)-4-trityloxy-2-butenyl]uracil
-
-
0.023
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
-
1
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
above
0.0022
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
-
-
0.26
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
-
-
0.0007
1-[2-(trityloxy)ethoxymethyl]uracil
-
-
0.017
1-[2-(trityloxy)ethoxymethyl]uracil
-
-
0.00004
1-[3-(tritylamino)propyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme K96A, at pH 8.0 and 25°
0.0002
1-[3-(tritylamino)propyl]pyrimidine-2,4(1H,3H)-dione
wild type enzyme, at pH 8.0 and 25°
0.0006
1-[3-(tritylamino)propyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme I117A, at pH 8.0 and 25°
0.028
1-[3-(tritylamino)propyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme F46A, at pH 8.0 and 25°
0.0025
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
-
-
1
1-[4-(tert-butoxycarbonylamino)-3-(trityloxymethyl)butyl]uracil
-
above
0.0013
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
-
-
0.074
1-[4-acetoxy-3-(tritylaminomethyl)butyl]uracil
-
-
0.0009
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
-
-
0.021
1-[4-hydroxy-2-(trityloxymethyl)butyl]uracil
-
-
0.00024
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
-
-
0.0057
1-[4-hydroxy-3-(tritylaminomethyl)butyl]uracil
-
-
0.00004
1-[4-hydroxy-3-[(tritylamino)methyl]butyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme K96A, at pH 8.0 and 25°
0.0002
1-[4-hydroxy-3-[(tritylamino)methyl]butyl]pyrimidine-2,4(1H,3H)-dione
wild type enzyme, at pH 8.0 and 25°
0.00027
1-[4-hydroxy-3-[(tritylamino)methyl]butyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme I117A, at pH 8.0 and 25°
0.029
1-[4-hydroxy-3-[(tritylamino)methyl]butyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme F46A, at pH 8.0 and 25°
0.00015
1-[6-(tritylamino)hexyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme K96A, at pH 8.0 and 25°
0.0018
1-[6-(tritylamino)hexyl]pyrimidine-2,4(1H,3H)-dione
wild type enzyme, at pH 8.0 and 25°
0.0044
1-[6-(tritylamino)hexyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme I117A, at pH 8.0 and 25°
0.035
1-[6-(tritylamino)hexyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme F46A, at pH 8.0 and 25°
0.0007
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
wild type enzyme, at pH 8.0 and 25°
0.008
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme I117A, at pH 8.0 and 25°
0.013
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
mutant enzyme F46A, at pH 8.0 and 25°
0.017
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.099
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
-
1
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
above
1
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
above
0.0048
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
mutant enzyme K96A, at pH 8.0 and 25°
0.005
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
-
pH 5.7-6.2, recombinant enzyme
0.005
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
wild type enzyme, at pH 8.0 and 25°
0.225
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
mutant enzyme F46A, at pH 8.0 and 25°
0.406
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
mutant enzyme I117A, at pH 8.0 and 25°
0.00011
2',5'-dideoxy-5'-(tritylamino)uridine
mutant enzyme K96A, at pH 8.0 and 25°
0.0002
2',5'-dideoxy-5'-(tritylamino)uridine
-
pH 5.7-6.2, recombinant enzyme
0.00024
2',5'-dideoxy-5'-(tritylamino)uridine
wild type enzyme, at pH 8.0 and 25°
0.0013
2',5'-dideoxy-5'-(tritylamino)uridine
mutant enzyme I117A, at pH 8.0 and 25°
0.02
2',5'-dideoxy-5'-(tritylamino)uridine
mutant enzyme F46A, at pH 8.0 and 25°
0.026
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
1
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
above
1
2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
above
0.067
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
0.232
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
-
1
3'-O-tert-butyldimethylsilyl-2',5'-dideoxyuridine 5'-N-diphenylphosphoramidate
-
above
0.088
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
0.324
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
-
1
3'-O-tert-butyldimethylsilyl-5'-O-sulfamoyl-2'-deoxyuridine
-
above
0.298
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C
0.547
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25°C, recombinant enzyme
0.058
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
0.298
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
0.433
5'-O-(1-adamantoyl)-2',3'-didehydro-2',3'-dideoxyuridine
-
-
0.082
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
0.799
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
1
5'-O-sulfamoylcarbamoyl-2',3'-didehydro-2',3'-dideoxyuridine
-
above
0.0013
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
0.35
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
-
1
5'-O-triphenylsilyl-2',3'-didehydro-2',3'-dideoxyuridine
-
above
0.975
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
-
1
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
above
1
5'-O-triphenylsilyl-2',3'-dideoxy-3'-fluorouridine
-
above
0.0028
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
0.909
5'-O-triphenylsilyl-2'-deoxyuridine
-
-
1
5'-O-triphenylsilyl-2'-deoxyuridine
-
above
0.189
5'-pentanoylamino-2',5'-dideoxyuridine
-
-
1
5'-pentanoylamino-2',5'-dideoxyuridine
-
above
1
5'-pentanoylamino-2',5'-dideoxyuridine
-
above
0.089
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
0.808
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
1
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
above
0.0002
5'-tritylamino-2',5'-dideoxyuridine
-
-
0.046
5'-tritylamino-2',5'-dideoxyuridine
-
-
0.304
5'-tritylamino-2',5'-dideoxyuridine
-
-
0.012
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
-
1
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
above
1
5'-tritylamino-3'-fluoro-2',3',5'-trideoxyuridine
-
above
0.0114
dUMP
-
pH 8.0, 25°C, recombinant enzyme
0.099
dUMP
-
pH 7.0, 25°C
0.115
dUTP
-
pH 7.0, 25°C, recombinant enzyme
0.121
dUTP
-
pH 7.0, 25°C, recombinant enzyme, without NaCl, presence of EDTA
additional information
2'-deoxy-5'-phenylmethylaminouracil
-
above 1 mM, pH 8.0, 25°C
additional information
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2',3'-dideoxyuracil
-
above 1 mM, pH 8.0, 25°C
additional information
5'-(2,3,3-trimethylbutan-2-yl)-3'-methyl-2',3'-dideoxyuracil
-
above 1 mM, pH 8.0, 25°C
additional information
5'-(2,4-dimethyl-3-(1-methylethyl)pentan-3-yl)-2'-deoxyuracil
-
above 1 mM, pH 8.0, 25°C
additional information
additional information
-
Ki of developed inhibitors higher than 1 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000026
(E)-3-(2,2-difluoroethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000033
(E)-3-(cyclopentyloxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000028
(E)-3-(cyclopropylmethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00034
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)-3-methoxybenzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0016
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.01
(R)-1-(4-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-yl)-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00041
(R)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00043
(R)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00082
(R)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000082
(R,E)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000041
(R,E)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000039
(R,E)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pent-3-ene-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-(3-[[(2S)-2-[hydroxy[bis(2-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-(3-[[(2S)-2-[hydroxy[bis(3-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00058
1-(4-[(2S)-2-[bis(3-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00035
1-(4-[(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-(4-[(2S)-2-[bis(4-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0006
1-(4-[(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0073 - 0.03
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
0.0094
1-[3-([(2R)-2-[hydroxy(diphenyl)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00028
1-[3-([(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00031
1-[3-([(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[3-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00015
1-[4-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[4-[(2S)-2-[bis[2-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[4-[(2S)-2-[bis[3-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.001
1-[4-[(2S)-2-[bis[4-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00023
1-[4-[(2S)-2-[hydroxy[di(thiophen-3-yl)]methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0042
1-[N-(2-triphenylmethylaminoethyl)-acetamide]uracil
Plasmodium falciparum
-
-
0.0025
1-[N-(3-triphenylmethylaminopropyl)-acetamide]uracil
Plasmodium falciparum
-
-
0.0029
1-[N-(4-triphenylmethylaminobutyl)-acetamide]uracil
Plasmodium falciparum
-
above
0.0039
1-[N-(triphenylmethyl) diaminodi(n-propyl) acetamide]uracil
Plasmodium falciparum
-
above
0.0045
1-[N-(triphenylmethylaminoethyl)-N-(aminoethyl) acetamide]uracil
Plasmodium falciparum
-
above
0.083
1-[N-hydroxyethyl-N-(triphenylmethylamino) ethyl-acetamide]uracil
Plasmodium falciparum
-
above
0.3
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.3 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0053
2',3',5'-trideoxy-3'-fluoro-5'-(tritylamino)uridine
Plasmodium falciparum
-
activity against the parasites with IC50: 0.0053 mM
0.002
2',3'-dideoxy-3'-fluoro-5'-O-trityluridine
Plasmodium falciparum
-
activity against the parasites with IC50: 0.0020 mM, binding structure involving Tyr112, Ile117, Ile108, and Asn103, overview
0.0045
2',5'-dideoxy-5'-(tritylamino)uridine
Plasmodium falciparum
-
activity against the parasites with IC50: 0.0045 mM
0.0011
2'-deoxy-5'-O-(triphenylsilyl)uridine
Plasmodium falciparum
-
activity against the parasites with IC50: 0.0011 mM
0.006
2'-deoxy-5'-O-trityluridine
Plasmodium falciparum
-
activity against the parasites with IC50: 0.006 mM
0.013
2'-deoxy-5'-O-[tris(1-methylethoxy)silyl]uridine
Plasmodium falciparum
-
activity against the parasites with IC50: 0.013 mM
0.015
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000073
3-(2,2-difluoroethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methylbutan-2-yl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylethyl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.022
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylhexan-3-yl)propanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-phenylpropyl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000031
3-(cyclopentyloxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000073
3-(cyclopropylmethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.000035
3-(cyclopropylmethoxy)-N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0025
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methyl-1,1-diphenylpropan-2-yl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methylpropan-2-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0013
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)-N-methylbutanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.016
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0011
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-hydroxy-2,2-diphenylethyl)-N-methylbutanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-1-phenylpropan-2-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.021
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-4-phenylbutan-2-yl)butanamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylpropan-2-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylpentan-3-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-phenylbutanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-[2-methyl-1-(naphthalen-2-yl)propan-2-yl]butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
N,N-dibenzyl-3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)propanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00127
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)-3-methoxybenzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0018
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
N-benzyl-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)butanamide
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00004
N-[(1R)-1-[3-(cyclopropylmethoxy)phenyl]ethyl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.074
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-D-alanyl-L-tyrosine
Trypanosoma cruzi
-
-
0.084
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-aspartic acid
Trypanosoma cruzi
-
-
0.081
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-glutamic acid
Trypanosoma cruzi
-
-
0.081
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-glutamine
Trypanosoma cruzi
-
-
0.081
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-lysine
Trypanosoma cruzi
-
-
0.087
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-threonine
Trypanosoma cruzi
-
-
0.1
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanylglycine
Trypanosoma cruzi
-
-
0.084
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-lysine
Trypanosoma cruzi
-
-
0.091
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-threonine
Trypanosoma cruzi
-
-
0.076
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-tyrosine
Trypanosoma cruzi
-
-
0.132
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycylglycine
Trypanosoma cruzi
-
-
0.00034
N-[2-[3-(cyclopropylmethoxy)phenyl]propan-2-yl]-3-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]propane-1-sulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.0046
N-[3-(tert-butyl diphenyl silanyloxy)-propyl]-2-uracil acetamide
Plasmodium falciparum
-
above
0.0037
N-[4-(tert-butyl diphenyl silanyloxy)-butyl]-2-uracil acetamide
Plasmodium falciparum
-
above
0.0039
N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.00003
Stl repressor protein from Staphylococcus aureus
Drosophila melanogaster
-
at pH 7.5 and 20°C
-
additional information
additional information
Trypanosoma cruzi
-
IC50 values of the inhibitor cytotoxicity assay on rat LC6 cells, overview
-
0.0073
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
0.03
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
apo state and in complex with dUMP, hanging drop vapor diffusion method, using 0.1 M ammonium citrate tribasic (pH 7.0), 12% (w/v) polyethylene glycol 3350 at 18°C (apoenzyme) or 0.1 M citric acid (pH 3.5), 14% (w/v) polyethylene glycol 1000 (enzyme in complex with dUMP)
in complex with dUMP and Mg2+, sitting drop vapor diffusion method, using 0.16 M sodium chloride, 0.08 M HEPES pH 7.5, 0.02 M sodium citrate tribasic dihydrate, 17% (w/v) polyethylene glycol 3350
hanging drop vapor diffusion method, using 50 mM Tris-HCl at pH 7.4 and 5 mM of the non-hydrolyzable ligand analog 2'-deoxyuridine 5'-[(alpha,beta)-imido]-triphosphate
purified recombinant enzyme, hanging drop vapour diffusion method, 25°C, 0.001 ml of protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.4, is mixed with 0.001 ml of reservoir solution containing 2 M ammonium sulfate and 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution, molecular replacement
in complex with dUMP. dU-PPi-Mg2+ triggers the ordering of both the C-terminal arm and a loop (residues 18-26) which is uniquely disordered in the Bacillus subtilis dUTPases. The dUMP complex suggests two stages in substrate release
isoform YncF complexed with dU-PPi-Mg2+. dU-PPi-Mg2+ triggers the ordering of both the C-terminal arm and a loop (residues 18-26) which is uniquely disordered in the Bacillus subtilis dUTPases. The dUMP complex suggests two stages in substrate release
purified recombinant selenomethionine-labelled YosS and YncF, hanging drop vapour diffusion method, for YosS: 30 mg/ml protein in 20 mM Tris-HCl, and 150 mM NaCl, pH 7.5, with 2.0 M ammonium sulfate, 0.2 M potassium/sodium tartrate, 0.1 M trisodium citrate, pH 5.6, in 3 days, for YncF: 20 mg/ml protein in 20 mM Tris-HCl, and 150 mM NaCl, pH 7.5, with 0.2 M trimethylamine N-oxide dehydrate, 15% w/v PEG MME 2000, 0.1 M Tris-HCl, pH 9.0, in two weeks, X-ray diffraction structure determination and analysis at 2.3 A and 1.7 A resolution, respectively
-
vapour diffusion method, cocrystallized with dUDP and Sr2+
-
hanging drop vapor diffusion method, using 12% (w/v) polyethylene glycol 4000, 10% (w/v) 2-propanol and 0.3 M sodium citrate pH 5.65 for the His-tagged enzyme, using 11% (w/v) polyethylene glycol 4000, 10% (w/v) 2-propanol and 0.3 M sodium citrate pH 5.65 for the His-tagged enzyme in complex with dUTP, or using 10% (w/v) polyethylene glycol 4000, 10% (w/v) 2-propanol and 0.3 M sodium citrate pH 5.6 for the mutant enzyme E81S/T84R in complex with dUTP
-
hanging and sitting drop vapor diffusion method, stable monomers observed in crystal phase
-
purified recombinant core enzyme lacking the 28-residue-long C-terminal fly-specific segment, sitting drop vapor diffusion method, 0.002 ml of 3 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.0, also containing 50 mM NaCl and 1 mM DTT, 1.2 mM dUDP and 10 mM MgCl2 are mixed with an equal volume of reservoir solution containing 50 mM sodium succinate buffer, pH 4.6-4.8, and 200 mM NaCl and 30-35% v/v 2-methyl-2,4-pentanediol, 4°C, X-ray diffraction structure determination and analysis at 1.88 A resolution
structure of dUTPase trimer, to 2.1 A resolution. The phage-specific insert folds into a small beta-pleated mini-domain reaching out from the dUTPase core surface. The insert mini-domains jointly coordinate a single Mg2+ ion per trimer at the entrance to the threefold inner channel. Residue Asp95, is the metal-ion-coordinating moiety potentially involved in correct positioning of the insert. The insert has no major role in dUTP binding or cleavage
Dubowvirus dv11
enzyme in complex with the substrate analogue dUDP
-
hanging-drop vapor diffusion method
purified recombinant enzyme in complex with inhibitors, i.e. dUTPase-alpha,beta-methylene-dUDP and dUTPase-dUDP-Mn complexes, 20°C, hanging-drop vapor diffusion, 3 mg/ml of enzyme in 10 mM Tris/HCl buffer, pH 7.0, and 50 mM NaCl, as well as 1.25 mM alpha,beta-methylene-dUDP or dUDP and 10 mM MgCl2 or MnCl2, respectively, mixing with an equal volume of reservoir solution 0.1 M Tris/HCl buffer, pH 7.8, containing 18-20% PEG 3350, and 400 mM Na-acetate, X-ray diffraction structure determination and analysis at 1.7-1.84 resolution, analysis of the different alpha-phosphate sites, overview
Q93H mutant in complex with a non-hydrolysable substrate analogue, alpha,beta-imido-dUTP, hanging drop vapor diffusion method, using 0.1 M Tris, 18-33.75 % polyethylene glycol 3350, 400 mM NaAc, pH 7.5
sitting drop vapor diffusion method, using 30% (w/v) PEG 1500
-
enzyme in complex with inhibitor alpha,beta-imino-dUTP and Mg2+, 0.282 mM dUTPase, 1.25 mM alpha,beta-imino-dUTP, and 10 mM MgCl2 in 10 mM Tris-HCl, 50 mM NaCl, and 0.1 mM TCEP, pH 7.0, are mixed with reservoir solution containing 0.1 M Na-HEPES buffer, pH 7.5, and 18-20% PEG 3350, generation of rhombohedral crystals, X-ray diffraction structure determination and analysis
purified recombinant enzyme
purified enzyme in complex with either product dUMPand Mg2+, or with substrate analogue alpha,beta-imino-dUTP, hanging drop vapour diffusion method, the reservoir solution contains 0.1 M Tris-HCl, pH 8.5, 20% PEG 3350, and 0.2 M LiSO4, a few weeks, soaking in europium nitrate solution, X-ray diffraction structure determination and analysis at 1.5A and 2.7 A resolution, respectively, single-wavelength anomalous diffraction
-
vapor diffusion method, using 0.3 M ammonium sulfate, 25% (w/v) polyethylene glycol 3350, 0.1 M HEPES, pH 7.0 (for mutant enzymes D131S/G78D and D131N), or using 150 mM malic acid, pH 7.5, and 25% (w/v) PEG 3350 (for mutant enzyme C4S), or using 0.1 M Tris, pH 8.5, 20% (w/v) polyethylene glycol 3350, 200 mM Li2SO4 (for mutant enzyme DELTAV, a 257-residue construct with the last 22 C-terminal residues removed)
in complex with nucleotides. Reaction starts with dUTPase capturing and properly positioning two substrates: dUTP and the catalytic water molecule. the catalytic water molecule is placed near the alpha-phosphate group opposite from the leaving group. Hydrolysis is then initiated by nucleophilic attack of Wthe water on the alpha-phosphate along the line of the scissile bond (in-line attack). A symmetric phosphorane-like transition state structure is formed with significant bond order in both forming and breaking bonds. Bond breaking is concomitant with inversion of the alpha-phosphate configuration and diphosphate-Mg2+ escape. The dUMP product then relaxes by rotation of the alpha-phosphate group and establishes a configuration similar to the one observed for this moiety in the E-S complex
O92810
purified recombinant C-terminal domain nucleocapsid fusion enzyme, hanging drop vapour diffusion method, 5 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 0.2 M NH4Cl, 10 mM MgCl2, 5 mM DTT, and 0.5 mM PMSF, with or without 1.3 mM alpha,beta-imino-dUTP, room temperature, mixed 1:1 with reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 8% w/v PEG 8000, X-ray diffraction structure determination and analysis at 1.75-2.3 A resolution
-
hanging drop vapor diffusion method, using 0.2 M potassium hydrogen phosphate and 20% (w/v) PEG3350 for mutant enzyme E145A complexed with alpha,beta-imido-dUTP, or 0.2 M potassium citrate and 20% (w/v) PEG3350 for mutant enzyme E145Q complexed with diphosphate
-
hanging drop vapor-diffusion method
dUTPase in complex with the isosteric substrate analogue, alpha,beta-imido-dUTP, and Mg2+, about 0.223 mM dUTPase, 1.25 mM alpha,beta-imido-dUTP and 10 mM MgCl2 in 10 mM Tris-HCl, pH7.0, 50 mM NaCl, and 0.1 mM TCEP buffer is mixed with different reservoir solutions, X-ray diffraction structure determination and analysis at 1.5 A resolution, molecular replacement
hanging and sitting drop vapor diffusion method
mutant enzymes D28N and T138STOP
mutant enzymes H145W and H145A in complex with alpha,beta-imido-dUTP, hanging drop vapor diffusion method, using 50 mM Tris-HCl pH 7.5, 10 mM MgCl2, 1.20-1.75 M ammonium sulfate and 10% (v/v) glycerol in a 1:1 ratio
mutant enzymes R140K/H145W and G143STOP, hanging drop vapor diffusion method, using 0.1 M Tris/HCl pH 7.5, 1.5 M ammonium sulfate, and 12.5% (v/v) glycerol
purified recombinant bifunctional dCTP deaminase:dUTPase in complex with inhibitor thymidine triphosphate, hanging drop vapor diffusion method, 15°C, 0.004 ml of enzyme solution containing 1.8 mg/ml enzyme, 20 mM MgCl2, 5 mM dTTP, 50 mM HEPES, pH 6.8, is mixed with 0.002 ml of reservoir solution, cotaining 45% PEG 400, 200 mM MgCl2 and 100 mM HEPES, pH 7.5, and equilibrated over 1 ml of reservoir solution, 1 day, for the free enzyme crystallization is used: 1.9 mg/ml enzyme and 50 mM HEPES, pH 6.8, mixed with 0.002 ml of reservoir solution, 20% PEG 8000, 50 mM MgCl2 and 100 mM HEPES, pH 7.5, and equilibrated over 1 ml of reservoir solution, for 1 day to 6 weeks, X-ray diffraction structure determination and analysis at 2.0-2.5 A resolution
purified recombinant enzyme in complex with inhibitor 2',3'-dideoxy-3'-fluoro-5'-O-trityluridine, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
hanging drop vapor diffusion method, apo-enzyme using 0.1 M ammonium sulfate, 0.1 M Bis-Tris (pH 5.5), and 25% (w/v) PEG3350. In complex with dUMP using 0.2 M sodium acetate, 0.1 M Tris-HCl (pH 8.5), and 30% (w/v) PEG4000. In complex with alpha,beta-imido dUTP using 30% Jeffamine ED-2001 (pH 7.0), 0.1 M potassium-HEPES (pH 7.0) and 3 mM MgCl2
purified recombinant free enzyme or recombinant enzyme complexed with substrate dUTP, hanging drop vapour diffusion method, protein and reservoir solution in a 1:1 ratio, 17°C, the reservoir solution contains 0.1 M HEPES, pH 7.5, 10% w/v PEG 8000, and 8% v/v ethylene glycol, 2 days, X-ray diffraction structure determination and analysis at 2.0 A resolution
Spbetavirus SPbeta
-
purified recombinant enzyme, sitting drop vapour diffusion method, 15 mg/ml protein in 20 mM Tris-HCl, and 150 mM NaCl, pH 7.5, with 0.2 M MgCl2, 25% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis at 1.3 A resolution
-
transition state analogue complexes in presence of dUMP, AlF3 and MgF3-. In the dimeric enzyme, the nucleophilic attack occurs on the beta-phosphate group
enzyme in complex with inhibitor dUDP, crystal structure determination and analysis
-
sitting drop vapor diffusion method, using 30% (w/v) PEG 1500
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D33A
the enzyme activity of the mutant is almost totally abolished
D91A
the enzyme activity of the mutant is almost totally abolished
F154A
the mutant exhibits approximately 10.5% of the activity of the wild type enzyme
Q120A
the enzyme activity of the mutant is almost totally abolished
R71A
the mutant exhibits approximately 9.6% of the activity of the wild type enzyme
S72A
the mutant exhibits approximately 6.5% of the activity of the wild type enzyme
Y94A
the mutant exhibits approximately 10% of the activity of the wild type enzyme
D48E/N57S
-
active site mutant
DELTA160-187
-
truncated form
D81A
Dubowvirus dv80alpha
mutant presents a 3fold reduced dUTP-binding capacity and an extremely low hydrolytic activity. Mutant is unable to induce transcription of the Stl-repressed SaPIbov1 genes even when expressed at a high level
D81N
Dubowvirus dv80alpha
mutant presents a 3fold reduced dUTP-binding capacity and an extremely low hydrolytic activity
Y84A
Dubowvirus dv80alpha
mutation of a strictly conserved residue. Mutant shows a reduced dUTP-binding capacity but retains some enzymatic activity
Y84F
Dubowvirus dv80alpha
mutation of a strictly conserved residue, mutant presents almost wild-type dUTP-binding capacity and activity
Y84I
Dubowvirus dv80alpha
mutation of a strictly conserved residue. Complete loss of dUTP-binding capacity
Q93H
the mutant enzyme is significantly inhibited by staphylococcal repressor StlSaPIbov1 protein (Ki 0.00000483 mM)
Q93R
the mutant enzyme is significantly inhibited by staphylococcal repressor StlSaPIbov1 protein (Ki 0.0000059 mM)
R116S
-
the mutant shows 5.2% of wild type activity
S72A
site-directed mutagenesis, steady-state kinetic characterization, S72A mutation causes a 725fold reduction in kcat and a 35fold reduction in KM.
T22R/R116S
-
the mutant shows 2.5% of wild type activity
D49N/F158W
-
the Asp/Asn mutation within motif I results in approximately 1000fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (4fold) whereas dUMP binding is only slightly affected
F158A
-
the mutant shows severely decreased catalytic activity compared to the wild type enzyme
C4S
the mutant shows increased activity compared to the wild type enzyme
D131E
the mutant is completely devoid of enzymatic activity
D131N
the mutant shows decreased activity compared to the wild type enzyme
D131S
the mutant shows decreased activity compared to the wild type enzyme
D131S/G78D
the mutant shows decreased activity compared to the wild type enzyme
F273A
the deletion of the flexible C-terminal tail carrying motif V results in a protein completely devoid of enzymatic activity
R268A
the mutant shows decreased activity compared to the wild type enzyme
E145A
-
the mutant shows reduced specific activity towards dUTP
E145Q
-
the mutant shows reduced specific activity towards dUTP
D28N/H145W
the Asp/Asn mutation within Motif I results in approximately 50fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (15fold) whereas dUMP binding is only slightly affected
G143STOP
the mutant shows severely reduced activity compared to the wild type enzyme
H145A
the mutant shows decreased catalytic activity compared to the wild type enzyme
R40K/H145W
the mutant shows severely reduced activity compared to the wild type enzyme
T138STOP
the mutant shows severely reduced activity compared to the wild type enzyme
D28N/H145W
-
the Asp/Asn mutation within Motif I results in approximately 50fold decrease of steady-state rate and significantly weakens the interaction of the protein with alpha,beta-imido-dUTP (15fold) whereas dUMP binding is only slightly affected
-
G143STOP
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
H145A
-
the mutant shows decreased catalytic activity compared to the wild type enzyme
-
R40K/H145W
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
T138STOP
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
F46A
the mutation does not affect the nucleotide hydrolase activity of dUTPase
I117A
the mutation does not affect the nucleotide hydrolase activity of dUTPase
K96A
the mutation does not affect the nucleotide hydrolase activity of dUTPase
D32A
the mutant exhibits negligible activity
D85A
the mutant exhibits negligible activity
D87A
the mutant exhibits negligible activity
F142A
the mutant exhibits very low activity
G82S
allele dut1-1 of gene dut1 possesses a single amino acid substitution in a conserved motif nearby the active site and exhibits a greatly reduced dUTPase activity, dut1-1 single mutant exhibits growth delay and cell cycle abnormalities and shows a strong spontaneous mutator phenotype, the dut1-1 allele is deleterious in wild-type strain and AP sites repair defective mutants, overview. The dut1-1 mutant is a spontaneous mutator that accumulates AT to CG transversions
Q114A
the mutant shows essentially the wild type affinity for dUTP and greatly reduced activity
R111A
the mutant has reduced activity and lower substrate affinity (increased Km) compared to the wild type enzyme
R137A
the mutant exhibits negligible activity
R68A
the mutant exhibits very low activity
S69A
the mutant exhibits negligible activity
Y88A
the mutant protein is equally active against both dUTP and UTP and has reduced activity and lower substrate affinity (increased Km) compared to the wild type enzyme
D170G
the mutant shows 68% of wild type activity
D170L
the mutant shows 1.7% of wild type activity
D34N
the mutant shows 1.6% of wild type activity
DELTA134-153
the mutant shows 0.73% of wild type activity
DELTA170-171
the mutant shows 14% of wild type activity
F166Y
the mutant shows 5.5% of wild type activity
K150A
the mutant shows 54% of wild type activity
K150E
the mutant shows 49% of wild type activity
R158A
the mutant shows 28% of wild type activity
R158E
the mutant shows 23% of wild type activity
R158W
the mutant shows 22% of wild type activity
R161K
the mutant shows 0.23% of wild type activity
R24T
the mutant shows 3.6% of wild type activity
R24T/S115R
the mutant shows 1.8% of wild type activity
R24T/S115R/D170G
the mutant shows 17% of wild type activity
S115R
the mutant shows 13% of wild type activity
V160D
the mutant shows 85% of wild type activity
E81S/T84R
-
the mutations lead to an increase in the optimal temperature of the enzyme to 55°C
E81S/T84R
-
the mutations lead to an increase in the optimal temperature of the enzyme to 55°C
-
D90N
site-directed mutagenesis
D90N
no effect on Km, strong decrease in catalytic activity, H-bonding significantly altered
F158W
site-directed mutagenesis, inactive mutant
F158W
-
the mutant shows decreased catalytic activity compared to the wild type enzyme
F158W
-
the mutation has no significant effect on the catalytic properties of dUTPase
H145W
site-directed mutagenesis, the replacement introduces a 244 sensitive fluorescent label into the binding site. The steady-state kinetics show no difference in the case of the mutant and wild-type enzyme
H145W
the mutant shows strongly reduced activity compared to the wild type enzyme
H145W
the mutant shows decreased catalytic activity compared to the wild type enzyme
H145W
the mutation has no significant effect on the catalytic properties of dUTPase
H145W
-
site-directed mutagenesis, the replacement introduces a 244 sensitive fluorescent label into the binding site. The steady-state kinetics show no difference in the case of the mutant and wild-type enzyme
-
H145W
-
the mutation has no significant effect on the catalytic properties of dUTPase
-
H145W
-
the mutant shows decreased catalytic activity compared to the wild type enzyme
-
H145W
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
additional information
removal of the physiologically present, very flexible 28-residue C-terminal segment does not perturb catalytic function but facilitates crystallization
additional information
mutations of a suggested hinge proline destabilize Escherichia coli dUTPase without preventing trimeric organization
additional information
-
mutations of a suggested hinge proline destabilize Escherichia coli dUTPase without preventing trimeric organization
additional information
increase in the expression of dUTPase in human lung and ovarian tumor cell lines is known to result in resistance to 5-fluorouracil
additional information
-
increase in the expression of dUTPase in human lung and ovarian tumor cell lines is known to result in resistance to 5-fluorouracil
additional information
-
overexpression of programmed cell death protein 4, Pdcd4, in a human endocrine pancreatic cell line Bon-1 decreases levels of dUTPase, but does not in colon carcinoma cell line HCT116, treatment of a human breast adenocarcinoma cell line MCF-7, with 5-fluorouracil results in regulated expression of Pdcd4 and dUTPase, overview
additional information
mutations of a suggested hinge proline destabilize human dUTPase without preventing trimeric organization. But trimer formation is prevented in the human enzyme by truncating the C-terminus before the swapping arm
additional information
-
mutations of a suggested hinge proline destabilize human dUTPase without preventing trimeric organization. But trimer formation is prevented in the human enzyme by truncating the C-terminus before the swapping arm
additional information
the DELTA-loop deletion mutant is created by deletion of the five (Ala133-Ser137) loop-specific amino acids and shows reduced kcat and increased Km values for dUTP
additional information
-
the DELTA-loop deletion mutant is created by deletion of the five (Ala133-Ser137) loop-specific amino acids and shows reduced kcat and increased Km values for dUTP
additional information
-
the DELTA-loop deletion mutant is created by deletion of the five (Ala133-Ser137) loop-specific amino acids and shows reduced kcat and increased Km values for dUTP
-
additional information
-
down-regulation of the enzyme activity by RNAi greatly reduces cell proliferation and increases the intracellular levels of dUTP. Defects in growth can be partially reverted by the addition of exogenous thymidine. dUTPase-depleted cells present hypersensitivity to methotrexate, a drug that increases the intracellular pools of dUTP, and enhanced uracil-DNA glycosylase activity, the first step in base excision repair, overview
additional information
-
down-regulation of the enzyme activity by RNAi greatly reduces cell proliferation and increases the intracellular levels of dUTP. Defects in growth can be partially reverted by the addition of exogenous thymidine. dUTPase-depleted cells present hypersensitivity to methotrexate, a drug that increases the intracellular pools of dUTP, and enhanced uracil-DNA glycosylase activity, the first step in base excision repair, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.