Information on EC 3.6.1.23 - dUTP diphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.6.1.23
-
RECOMMENDED NAME
GeneOntology No.
dUTP diphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
mechanism
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
mechanism
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
catalytic mechanism
P9WNS5
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
active site structure, R84 and S81 are involved in substrate binding, molecular modeling
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
product and substrate active site binding structure, catalytic mechanism of the monomeric enzyme in comparison to trimeric dUTPases, overview
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
structural and catalytic mechanism
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
structural and catalytic mechanism involving Mg2+
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
structural organization and substrate binding modes
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
catalytic reaction mechanism, overview
-
dUTP + H2O = dUMP + diphosphate
show the reaction diagram
structural organization and substrate binding modes, catalytic mechanism
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
pyrimidine deoxyribonucleotides de novo biosynthesis I
-
-
pyrimidine deoxyribonucleotides de novo biosynthesis II
-
-
pyrimidine deoxyribonucleotides de novo biosynthesis III
-
-
pyrimidine deoxyribonucleotides dephosphorylation
-
-
Pyrimidine metabolism
-
-
pyrimidine metabolism
-
-
superpathway of pyrimidine deoxyribonucleotides de novo biosynthesis (E. coli)
-
-
SYSTEMATIC NAME
IUBMB Comments
dUTP nucleotidohydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
desoxyuridine 5'-triphosphatase
-
-
-
-
desoxyuridine 5'-triphosphate nucleotidohydrolase
-
-
-
-
desoxyuridine-triphosphatase
-
-
-
-
dUTP pyrophosphatase
-
-
-
-
dUTPase
-
-
-
-
P18
-
-
-
-
PIP4
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37289-34-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acholeplasma laidlawii B-PG9
B-PG9
-
-
Manually annotated by BRENDA team
genes yncF and yosS
-
-
Manually annotated by BRENDA team
Chlorella virus IL-3A
-
-
-
Manually annotated by BRENDA team
two dUTPase isozymes
-
-
Manually annotated by BRENDA team
two isozymes
-
-
Manually annotated by BRENDA team
overproducing strain
-
-
Manually annotated by BRENDA team
Escherichia coli overproducing
overproducing strain
-
-
Manually annotated by BRENDA team
Escherichia coli R2
R2
-
-
Manually annotated by BRENDA team
after infection with herpes simplex type 1 virus a distinct species of dUTPase is induced in HeLa S3 cells
-
-
Manually annotated by BRENDA team
gene DUT; gene DUT
SwissProt
Manually annotated by BRENDA team
HSV-1-induced dUTPase and KB dUTPase
-
-
Manually annotated by BRENDA team
EBV, strain B95-8, gene BLLF3
-
-
Manually annotated by BRENDA team
M-PMV, a beta-retrovirus
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis mc2155
-
UniProt
Manually annotated by BRENDA team
subsp. mycoides
-
-
Manually annotated by BRENDA team
no activity in caprine lentivirus genotype E
-
-
-
Manually annotated by BRENDA team
strain 3D7
-
-
Manually annotated by BRENDA team
Pyrococcus woesei DSM 3773
-
UniProt
Manually annotated by BRENDA team
RGV, an iridovirus pathogenic in the pig frog
-
-
Manually annotated by BRENDA team
several strains, overview, gene DUT1
SwissProt
Manually annotated by BRENDA team
WSSV, ORF wsv112 or gene wdut
-
-
Manually annotated by BRENDA team
Sulfolobus islandicus rod-shaped virus SIRV
Uniprot
Manually annotated by BRENDA team
strain NA1
SwissProt
Manually annotated by BRENDA team
strain 427, gene DUT with T49 and E248
-
-
Manually annotated by BRENDA team
Trypanosoma brucei 427
strain 427, gene DUT with T49 and E248
-
-
Manually annotated by BRENDA team
DURP gene, several different virus of the alpha-, beta-, and gammaherpesviridae, e.g. HSV-1, HHV-8, or HCMV, overview
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
lack of dUTPase leads to uracil-substituted DNA that perturbs base excision repair, resulting in DNA fragmentation and thymine-less cell death
malfunction
A0QW08
dUTPase knock-out results in lethality
malfunction
Mycobacterium smegmatis mc2155
-
dUTPase knock-out results in lethality
-
physiological function
-
dUTPase is responsible for prevention of uracil incorporation into DNA
physiological function
-
the enzyme is involved in nucleotide metabolism that acts as first line of defence against uracil incorporation into DNA
physiological function
P33317
the enzyme plays a key role in preventing uracil incorporation into DNA
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-dideoxyUTP + H2O
2',3'-dideoxy-UMP + diphosphate
show the reaction diagram
-
76% of the activity with dUTP
-
-
?
2'-deoxy-5-fluoro-UTP + H2O
2'-deoxy-5-fluoro-UMP + diphosphate
show the reaction diagram
-
most specific substrate
-
-
?
6-azaUTP + H2O
6-azaUMP + diphosphate
show the reaction diagram
-
39% of the activity with dUTP
-
-
?
araUTP + H2O
araUMP + diphosphate
show the reaction diagram
-
90% of the activity with dUTP
-
-
?
beta-L-2'-dUTP + H2O
beta-L-2'-dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dATP + H2O
dAMP + diphosphate
show the reaction diagram
-
-
-
-
?
dATP + H2O
dAMP + diphosphate
show the reaction diagram
-
low activity
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
A7J1X3
-
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
-
no activity
-
-
-
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
-
low activity
-
-
?
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
A7J1X3
about 10fold lower activity with dCTP compared to dUTP
-
-
?
dGTP + H2O
dGMP + diphosphate
show the reaction diagram
-
-
-
-
?
dGTP + H2O
dGMP + diphosphate
show the reaction diagram
-
low activity
-
-
?
dITP + H2O
dIMP + diphosphate
show the reaction diagram
P33317
shows also significant activity against dITP
-
-
?
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
-
-
-
-
?
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
Q57872
-
-
-
?
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
-
no activity
-
-
-
dTTP + H2O
dTMP + diphosphate
show the reaction diagram
-
low activity
-
-
?
dUDP + H2O
dUMP + phosphate
show the reaction diagram
-
-
-
-
?
dUDP + H2O
dUMP + phosphate
show the reaction diagram
-
-
-
-
?
dUDP + H2O
deoxyuridine + diphosphate
show the reaction diagram
-
the enzyme is highly specific for deoxyuridine nucleotides
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P06968
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P33316
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Q9STG6
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
O71028
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Q57872
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P33316
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P33317
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P03195
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
A0QW08
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Q8II92
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
A7J1X3
preferred substrate
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
most specific substrate
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P06968
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q57872
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
show the reaction diagram
-
biological roles and functions of dUTPase-related proteins and domains, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUMP is required for biosynthesis of dTTP, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is essential in the lytic cycle of the virus
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme regulates the levels of dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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, substrate binding structure analysis, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is highly specific for dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
dUTPase is essential for DNA integrity and is an important survival factor for cancer cells
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUTPase is essential in controlling relative cellular levels of dTTP/dUTP, both of which can be incorporated into DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
enzyme inhibition is involved in apoptosis in cancer cells and decreases the sensitivity of cells for 5-fluorouracil, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
Q9STG6
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
show the reaction diagram
A7J1X3
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
show the reaction diagram
-
development of a robust and continuous dUTPase enzyme activity assay method using phenolred indicator, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
substrate binding structure, the strictly conserved residue Ser72 is involved in phosphate chain binding, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
dUTPase catalyzes the hydrolysis of dUTP to dUMP and diphosphate controlling the incorporation of uracil into DNA genomes
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
dUTPase catalyzes the hydrolysis of the alpha,beta-diphosphate bond of dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is highly specific for deoxyuridine nucleotides
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Mycobacterium smegmatis mc2155
A0QW08
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Chlorella virus IL-3A
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Escherichia coli overproducing
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Acholeplasma laidlawii B-PG9
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Acholeplasma laidlawii B-PG9
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis, development of a robust and continuous dUTPase enzyme activity assay method using phenolred indicator, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Trypanosoma brucei 427
-
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
show the reaction diagram
Escherichia coli R2
-
-
-
?
dUTP + H2O
?
show the reaction diagram
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
-
dUTP + H2O
?
show the reaction diagram
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
?
dUTP + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme prevents a deleterious incorporation of uracil into DNA
-
-
?
dUTP + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
enzyme plays a key role in deoxyribonucleotide metabolism
-
-
-
dUTP + H2O
?
show the reaction diagram
P33316
enzyme is important in DNA replication
-
-
?
dUTP + H2O
?
show the reaction diagram
-
enzyme is involved in controlling intracellular dUTP levels
-
-
?
dUTP + H2O
?
show the reaction diagram
-
enzyme of pyrimidine deoxyribonucleotide metabolism
-
-
?
dUTP + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
Acholeplasma laidlawii B-PG9
-
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
-
-
?
UTP + H2O
UMP + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + diphosphate
show the reaction diagram
-
at about 3% of the activity with dUTP
-
-
?
UTP + H2O
UMP + diphosphate
show the reaction diagram
P33317
substrate for mutant enzyme Y88A
-
-
?
dUTPalphaS + H2O
dUMP + thiodiphosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no hydrolysis of dUDP
-
-
-
additional information
?
-
-
comparison of the Drosophila melanogaster and the Escherichia coli enzymes
-
-
-
additional information
?
-
-
substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
-
additional information
?
-
-
the enzyme binds non-cooperatively to 2'-dUMP
-
-
-
additional information
?
-
-
overexpression of dUTPase is associated with resistance to chemotherapeutic agents targeting thymidilate biosynthesis
-
-
-
additional information
?
-
A7J1X3
the enzyme is essential for survival
-
-
-
additional information
?
-
P9WNS5
the bifunctional dCTP deaminase:dUTPase shows very similar affinities for dCTP and deoxyuridine triphosphate as substrates, overview
-
-
-
additional information
?
-
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
-
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
?
-
-
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
?
-
P33317
alpha,beta-imido dUTP is a non-hydrolysable substrate
-
-
-
additional information
?
-
-
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
-
additional information
?
-
Mycobacterium smegmatis, Mycobacterium smegmatis mc2155
A0QW08
the enzyme cannot hydrolyze alpha-beta-imido-dUTP
-
-
-
additional information
?
-
-
biological functions in housekeeping, overview, substrate specificity, no hydrolysis of canonical NTPs, overview
-
-
-
additional information
?
-
P9WNS5
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
?
-
Trypanosoma brucei 427
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dCTP + H2O
dCMP + diphosphate
show the reaction diagram
A7J1X3
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P33316
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
A0QW08
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Q8II92
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P06968
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q57872
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
show the reaction diagram
-
biological roles and functions of dUTPase-related proteins and domains, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUMP is required for biosynthesis of dTTP, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
the enzyme is essential in the lytic cycle of the virus
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme regulates the levels of dUTP
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
dUTPase is essential for DNA integrity and is an important survival factor for cancer cells
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUTPase is essential in controlling relative cellular levels of dTTP/dUTP, both of which can be incorporated into DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
enzyme inhibition is involved in apoptosis in cancer cells and decreases the sensitivity of cells for 5-fluorouracil, overview
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
Q9STG6
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
show the reaction diagram
A7J1X3
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
dUTPase catalyzes the hydrolysis of dUTP to dUMP and diphosphate controlling the incorporation of uracil into DNA genomes
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
-
dUTP + H2O
?
show the reaction diagram
-
enzyme suppresses incorporation of uracil into DNA and provides a pool of dUMP, the precursor of dTTP
-
-
?
dUTP + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme prevents a deleterious incorporation of uracil into DNA
-
-
?
dUTP + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
enzyme plays a key role in deoxyribonucleotide metabolism
-
-
-
dUTP + H2O
?
show the reaction diagram
P33316
enzyme is important in DNA replication
-
-
?
dUTP + H2O
?
show the reaction diagram
-
enzyme is involved in controlling intracellular dUTP levels
-
-
?
dUTP + H2O
?
show the reaction diagram
-
enzyme of pyrimidine deoxyribonucleotide metabolism
-
-
?
dUTP + H2O
?
show the reaction diagram
-
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
dUMP + diphosphate
show the reaction diagram
Mycobacterium smegmatis mc2155
A0QW08
-
-
-
?
dUTP + H2O
?
show the reaction diagram
Acholeplasma laidlawii B-PG9
-
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
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
P9WNS5
removes dUTP from the nucleotide triphosphate pool and therefore prevents the incorporation of uracil into the DNA
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
dUTPase is essential to eliminate dUTP for DNA integrity and provide dUMP for thymidylate biosynthesis
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
Trypanosoma brucei 427
-
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
-
-
?
additional information
?
-
-
overexpression of dUTPase is associated with resistance to chemotherapeutic agents targeting thymidilate biosynthesis
-
-
-
additional information
?
-
A7J1X3
the enzyme is essential for survival
-
-
-
additional information
?
-
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
-
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
?
-
-
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
?
-
-
biological functions in housekeeping, overview
-
-
-
additional information
?
-
Trypanosoma brucei 427
-
procyclic cells with reduced dUTPase activity exhibit an altered cell cycle and DNA fragmentation
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
can partially replace Mg2+, causes increase in Km
Co2+
-
activates to 72% of the activity with Mg2+
Co2+
-
can substitute the physiological cofactor Mg2+, however the kcat is significantly reduced compared to dUTP-Mg2+
Co2+
P33317
strictly dependent on a bivalent metal cation like Co2+
Mg2+
-
slight stimulation at low concentrations of dUTP, no stimulation at concentrations of dUTP above 0.1 mM
Mg2+
-
no requirement for Mg2+
Mg2+
-
MgCl2 stimulates
Mg2+
-
no requirement for Mg2+
Mg2+
-
maximal activity in presence of 0.04 mM Mg2+
Mg2+
-
enhances activity
Mg2+
-
dialyzed enzyme is activated 2fold by 5 mM MgCl2, reverses inhibition by EDTA
Mg2+
-
stimulates, enzyme also exhibits activity in absence of divalent cations
Mg2+
-
0.5 mM, stimulates by 7%; metalloenzyme, may contain Mg2+, Mn2+ or both
Mg2+
-
molar ratio of Mg2+ to tetrameric dUTPase is 0.08-0.1
Mg2+
-
dependent on Mg2+ or Mn2+ for optimal activity, maximal activity at 25 mM Mg2+
Mg2+
-
Mg2+ enhances binding to dUTPase of dUTP by a factor of 100 and dUDP by a factor of 10
Mg2+
-
Mg2+, Mn2+ or Zn2+ required for enzyme function
Mg2+
Q57872
required
Mg2+
-
required, modulates conformation of the enzyme
Mg2+
-
required for stabilization of the active form of the enzyme
Mg2+
-
required, three ions per subunit
Mg2+
-
required, no activity in the absence of Mg2+
Mg2+
-
best divalent cation, bound at the center of the trimeric enzyme structure
Mg2+
-
binding as dUTP-Mg2+ at the C-terminus induces the closure of the C-terminal arm
Mg2+
-
binding as dUTP-Mg2+ at the C-terminus induces the closure of the C-terminal arm which opens up again after hydrolysis to expel the product
Mg2+
-
required, best divalent cation
Mg2+
-
binding structure, Mg2+ does not bind in the active site
Mg2+
-
required, binding structure, overview
Mg2+
-
required
Mg2+
-
activates, phosphate chain coordination involves Mg2+, binding structure, overview. Mg2+ probably dissociates from the enzyme with the product PPi and not with dUMP
Mg2+
-
activates
Mg2+
-
dependent on, the energetic barrier of the reaction is 4fold higher when Mg2+ is depleted
Mg2+
-
dependent on
Mg2+
-
required
Mg2+
-
required for activity
Mg2+
-
required for full activity, In the absence of divalent cations, dUTPase retains about 50% of the catalytic rate observed in the presence of Mg2+
Mg2+
P03195
required, Mg2+ plays a role mainly in substrate binding
Mg2+
P33317
strictly dependent on a bivalent metal cation like Mg2+ which supports the highest rate of dUTP hydrolysis
Mn2+
-
metalloenzyme, may contain Mg2+, Mn2+ or both
Mn2+
-
dependent on Mg2+ or Mn2+ for optimal activity
Mn2+
-
Mg2+, Mn2+ or Zn2+ required for enzyme function
Mn2+
-
can replace for Mg2+
Mn2+
-
can partially replace Mg2+, causes increase in Km
Mn2+
-
activates to 68% of the activity with Mg2+
Mn2+
-
can substitute the physiological cofactor Mg2+, however the kcat is significantly reduced compared to dUTP-Mg2+
Mn2+
P33317
strictly dependent on a bivalent metal cation like Mn2+
NaCl
-
maximal activity at 0.1 M
Ni2+
-
activates to 49% of the activity with Mg2+
Ni2+
P33317
strictly dependent on a bivalent metal cation like Ni2+
VO2+
-
results a higher activity than Mg2+ or Mn2+
Zn2+
-
appears to be essential for activity
Zn2+
-
0.5 mM, stimulates by 7%
Zn2+
-
Mg2+, Mn2+ or Zn2+ required for enzyme function
Zn2+
P33317
strictly dependent on a bivalent metal cation like Zn2+
additional information
-
no effect by Zn2+
additional information
A7J1X3
the enzymatic activity of the dUTPase is largely unaffected by variations in MgCl2, KCl, (NH4)2SO4, and Triton X-100 concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
-
-
1,10-phenanthroline
-
50 mM, 30% inhibition
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
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-(tritylamino)propyl]pyrimidine-2,4(1H,3H)-dione
-
-
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
-
-
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
-
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'-deoxy-5'-O-(triphenylsilyl)uridine
-
activity against the parasites with IC50: 0.0011 mM
2'-deoxy-5'-O-trityluridine
-
activity against the parasites with IC50: 0.006 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
-
-
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
best inhibitor
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{[hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl)uridine
-
competitive inhibition
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
-
-
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'-pentanoylamino-2',5'-dideoxyuridine
-
-
5'-tert-butyldiphenylsilyloxy-2',3'-dideoxy-3'-fluorouridine
-
-
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-dUDP
-
-
alpha,beta-imido-dUDP
-
potent inhibition
alpha,beta-imido-dUTP
-
substrate analogue, inhibits the wild-type enzyme, not mutant S72A
alpha,beta-imido-dUTP
-
competitive inhibition
alpha,beta-imido-dUTP
-
-
alpha,beta-imido-dUTP
-
-
alpha,beta-imido-dUTP
-
-
alpha-beta-imido-dUTP
-
competitive, strong inhibition
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
A7J1X3
38% inhibition at 0.01%
-
Ca2+
-
5 mM, 69% inhibition
Cu2+
-
0.5 mM, 50% inhibition
Cu2+
-
-
diphosphate
-
-
dTTP
Q57872
competitive feedback inhibition
dUDP
-
competitive
dUDP
-
binding structure
dUDP
-
competitive inhibition
dUMP
-
competitive
dUMP
-
product inhibition
dUMP
-
product, competitive inhibition
dUMP
-
product inhibition
dUMP alphaS
-
-
dUTP
-
substrate inhibition at higher concentrations
dUTPalphaS
-
-
-
EDTA
-
2 mM, complete inhibition
EDTA
-
reversed by Mg2+ or Zn2+
EDTA
-
-
EDTA
-
1 mM, 91% inhibition
EDTA
-
0.5 mM, more than 90% inhibition
EDTA
-
dissociation of the enzyme into its monomeric form
EDTA
-
reversed by Mg2+, Mn2+, Zn2+, Co2+ and Ca2+
EDTA
-
reversed by Mg2+, Co2+ or Mn2+
EDTA
-
reversed by Co2+ or Mg2+
EDTA
-
reversed by Mg2+, Mn2+ or Zn2+
EDTA
-
1 mM, 65% loss of activity
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
P33317
less than 10% residual activity at 1 mM
EGTA
-
10 mM, more than 90% inhibition
EGTA
-
-
fluorodeoxy-UMP
-
-
-
guanidine hydrochloride
-
kinetics of GuHCl-induced denaturation of the two dUTPase isozymes at pH 7.5, 4 C and 1.5-4 M
Hg2+
-
10 mM HgCl2, 50% inhibition in absence of mercaptoethanol
Hydroxymercuribenzoate
-
5 mM, complete inhibition
-
KCl
-
0.4 mM, 29% loss of activity
Mg2+
-
complete inhibition by extensive dialysis against 0.0125 M MgCl2
Mn2+
-
5 mM, 26% inhibition
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
P33316
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
-
thymidine 5'-(alpha,beta-imido)triphosphate
-
-
thymidine triphosphate
P9WNS5
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
Uracil
-
5 mM, 30% loss of activity
Zn2+
-
5 mM, 23% inhibition
Zn2+
-
-
additional information
-
diphosphate has no effect on activity
-
additional information
-
inhibitor in vivo activity against the parasite, overview
-
additional information
-
growth inhibition potency in vitro, overview, molecular docking modeling study
-
additional information
-
no inhibition by dTTp, dGTP, dATP, and dCTP
-
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
-
binding of alpha,beta-imino-dUTP does not induce allosteric conformational changes and does not protect the enzyme against tryptic digestion
-
additional information
-
programmed cell death protein 4 downregulates dUTPase in certain cell types, overview
-
additional information
-
fast screening for binding of potential inhibitors to the active site
-
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
-
computational docking of small molecules structures to the enzyme for inhibitor development, overview
-
additional information
-
design and synthesis of tert-butyl diphenyl silyl uracil acetamides inhibitors, molecular modelling, overview
-
additional information
-
several dUMP analogues with substituents at the 3'- or 5'-positions show poor inhibitory activity
-
additional information
-
the enzyme is not inhibited by 3'-azido-2',3'-dideoxy-UTP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
50-500 mM, 25% stimulation
bis(acetylacetonato)oxovanadium(IV)
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00173
2'-deoxy-5-fluoro-UTP
-
at 25C 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 25C 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 25C 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 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
1.13
dATP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.465
dCTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.687
dCTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
2.3
dCTP
-
pH 7.5, 25C
1.96
dGTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0447
dITP
P33317
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
0.29
dTTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.64
dTTP
-
pH 7.5, 25C
0.761
dTTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0062
dUDP
-
25C
0.025
dUDP
-
-
0.0627
dUDP
-
pH 8, 25C
0.13
dUDP
-
-
0.17
dUDP
-
-
0.0001
dUTP
-
-
0.00017
dUTP
-
pH and temperature not specified in the publication
0.00018
dUTP
-
-
0.00022
dUTP
-
pH and temperature not specified in the publication
0.0003
dUTP
-
-
0.0004
dUTP
-
pH 7.5, 25C
0.0005
dUTP
-
25C
0.0006
dUTP
-
pH 7.5, 25C, recombinant enzyme
0.0006
dUTP
P03195
mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.00066
dUTP
-
pH 8.0, 25C, recombinant enzyme
0.0007
dUTP
-
pH 7.6, 25C, recombinant enzyme, in presence of 1 mM MgCl2
0.00071
dUTP
P03195
wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.0008
dUTP
P03195
wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.0009
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20C
0.00094
dUTP
-
-
0.00096
dUTP
-
pH and temperature not specified in the publication
0.001
dUTP
-
-
0.001
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
0.0011
dUTP
-
pH 6.2-8.0
0.0011
dUTP
-
at 25C 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 20C
0.0012
dUTP
-
recombinant enzyme
0.0015
dUTP
-
in presence of Mg2+, at low concentrations of dUTP
0.0016
dUTP
-
wild type enzyme, at pH 8.0 and 25C
0.0017
dUTP
-
mutant enzyme I117A, at pH 8.0 and 25C
0.00179
dUTP
-
pH 7.4, 37C, recombinant enzyme
0.0018
dUTP
-
mutant enzyme F46A, at pH 8.0 and 25C
0.00187
dUTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0019
dUTP
-
pH 7.0, 25C, recombinant enzyme
0.0019
dUTP
-
mutant enzyme K96A, at pH 8.0 and 25C
0.002
dUTP
-
-
0.0021
dUTP
-
pH 8, 25C
0.0024
dUTP
-
pH 5.7-6.2, recombinant enzyme
0.0025
dUTP
-
enzyme form DUT-N and DUT-M
0.003
dUTP
-
-
0.0036
dUTP
-
-
0.0036
dUTP
-
pH 7.4, 20C, 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 20C
0.0037
dUTP
-
in presence of 1 mM Mg2+
0.004
dUTP
-
in absence of Mg2+, at low concentrations of dUTP
0.004
dUTP
-
enzyme from uninfected KB cells
0.0045
dUTP
-
-
0.0045
dUTP
-
-
0.0048
dUTP
-
enzyme from herpes simplex virus type 1 infected KB cells
0.0052
dUTP
P03195
mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.0052
dUTP
-
mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
0.006
dUTP
-
-
0.006
dUTP
P03195
wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.007
dUTP
P03195
mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.008
dUTP
-
-
0.008
dUTP
P03195
mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.009
dUTP
P03195
mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.0117
dUTP
-
pH 8.5, 50C, recombinant enzyme
0.012
dUTP
-
-
0.0132
dUTP
P33317
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
0.0142
dUTP
P33317
mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
0.016
dUTP
-
-
0.0315
dUTP
P33317
mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
0.041
dUTP
P33317
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
0.45
dUTP
-
D90N mutant enzyme, pH 7.8, room temperature
0.5
dUTP
-
wild-type enzyme, pH 7.8, room temperature
0.0027
dUTP-Co2+
-
pH 7.0, 25C, recombinant enzyme
0.0019
dUTP-Mg2+
-
pH 7.0, 25C, recombinant enzyme
0.0137
dUTP-Mn2+
-
pH 7.0, 25C, recombinant enzyme
0.035
UTP
P33317
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
0.54
UTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.571
UTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
0.0002
dUTPalphaS
-
-
-
additional information
additional information
Q57872
lower affinity for dUTP than strict dUTPases
-
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
-
kinetics of dUTP binding
-
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
P9WNS5
steady-state kinetic analysis of the dual activities of the bifunctional enzyme, overview
-
additional information
additional information
-
ligand binding constants
-
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
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.4
dATP
-
pH 8, 25C
0.7
dCTP
-
pH 7.5, 25C
13
dCTP
-
pH 8, 25C
6.4
dGTP
-
pH 8, 25C
1.3
dITP
P33317
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
0.1
dTTP
-
pH 7.5, 25C
8.6
dTTP
-
pH 8, 25C
65
dUDP
-
pH 8, 25C
0.0003
dUTP
-
D90N mutant enzyme, pH 7.8, room temperature
0.007
dUTP
-
mutant enzyme D49N/F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
0.024
dUTP
-
mutant enzyme D28N/H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
0.04
dUTP
P03195
mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C; mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.06
dUTP
P03195
mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.18
dUTP
P03195
mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
0.32
dUTP
-
mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
0.88
dUTP
-
DELTA-loop mutant enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20C
1.2
dUTP
-
mutant enzyme H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
1.2
dUTP
P03195
wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
1.22
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20C
1.3
dUTP
P33317
mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
1.4
dUTP
P03195
wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
1.6
dUTP
P03195
wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
1.7
dUTP
P03195
mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
2.8
dUTP
-
25C
3.3
dUTP
-
pH 7.6, 25C, recombinant enzyme, in presence of 1 mM MgCl2
3.3
dUTP
P33317
mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
3.4
dUTP
-
pH 7.0, 25C, recombinant enzyme
3.7 - 5.8
dUTP
-
pH 7.5, 25C, recombinant wild-type and mutant enzymes
4.5
dUTP
-
pH 7.5, 25C, in the absence of added metal ions
5 - 15
dUTP
-
-
5.8 - 6.2
dUTP
-
-
5.8
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
6 - 9
dUTP
-
-
6.3
dUTP
-
mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
6.58
dUTP
-
pH 7.4, 20C, recombinant wild-type enzyme
6.8
dUTP
-
pH 8.5, 50C, recombinant enzyme
6.8
dUTP
-
mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
7.4
dUTP
P33317
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
8
dUTP
-
recombinant wild-type and mutant enzymes
9.17
dUTP
-
-
9.6
dUTP
P33317
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
9.7
dUTP
-
pH 7.4, 37C, recombinant enzyme
11
dUTP
-
wild-type enzyme, pH 7.8, room temperature
11.33
dUTP
-
mutant enzyme F46A, at pH 8.0 and 25C
11.67
dUTP
-
mutant enzyme K96A, at pH 8.0 and 25C; wild type enzyme, at pH 8.0 and 25C
12
dUTP
-
pH 7.5, 25C
12
dUTP
-
mutant enzyme I117A, at pH 8.0 and 25C
12.3
dUTP
-
pH 8.0, 25C, recombinant enzyme
14.7
dUTP
-
pH 7.5, 25C, in the presence of Mg2+ or Mn2+
18
dUTP
-
pH 7.5, 25C, recombinant enzyme
24.2
dUTP
-
pH 7.5, 25C, in the presence of bis(acetylacetonato)oxovanadium(IV)
27.3
dUTP
-
pH 7.5, 25C, in the presence of VO2+ or bis(acetylacetonato)oxovanadium(IV)
38.3
dUTP
-
at 30C
49
dUTP
-
pH 8, 25C
58.3
dUTP
-
at 35C
4.1
dUTP-Co2+
-
pH 7.0, 25C, recombinant enzyme
13.3
dUTP-Mg2+
-
pH 7.0, 25C, recombinant enzyme
5.3
dUTP-Mn2+
-
pH 7.0, 25C, recombinant enzyme
5.3
UTP
P33317
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
110
2'-deoxy-5-fluoro-UTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
41379
600
2'-deoxy-5-fluoro-UTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
41379
0.00525
beta-L-2'-dUTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
41380
0.0061
beta-L-2'-dUTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
41380
0.00265
dATP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
140
0.02172
dCTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
179
0.1616
dCTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
179
0.00013
dGTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
219
29
dITP
P33317
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
2839
0.0092
dTTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
145
0.01971
dTTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
145
6
dUTP
P03195
mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
435
8
dUTP
P03195
mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C; mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
435
20
dUTP
P03195
mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
435
62
dUTP
-
mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
435
90
dUTP
P33317
mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
435
100
dUTP
P33317
mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
435
180
dUTP
P33317
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
435
200
dUTP
P03195
wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
435
740
dUTP
P33317
wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
435
1800
dUTP
P03195
wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
435
1900
dUTP
-
mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
435
2300
dUTP
P03195
wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
435
2800
dUTP
P03195
mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25C
435
5800
dUTP
-
wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20C
435
6100
dUTP
-
mutant enzyme K96A, at pH 8.0 and 25C
435
6300
dUTP
-
mutant enzyme F46A, at pH 8.0 and 25C
435
6600
dUTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
435
7100
dUTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
435
7100
dUTP
-
mutant enzyme I117A, at pH 8.0 and 25C
435
7300
dUTP
-
wild type enzyme, at pH 8.0 and 25C
435
0.01121
UTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
65
0.01278
UTP
-
at 25C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0
65
150
UTP
P33317
mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30C
65
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
0.0033
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 37C
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
-
-
0.005
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-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
-
1
1-[2-(azidomethyl)-4-(trityloxy)butyl]uracil
-
above
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
1-[2-(hydroxymethyl)-4-(trityloxy)butyl]uracil
-
-
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
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
0.0373
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
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 37C
0.0125
2',3',5'-trideoxy-3'-fluoro-5'-(tritylamino)uridine
-
pH 5.7-6.2, recombinant enzyme
0.099
2',3'-didehydro-2',3'-dideoxyuridine 5'-diphenyl phosphate
-
-
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
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
0.908
2'-deoxy-5'-triphenylmethanyluracil
-
pH 8.0, 25C
0.135
2'-deoxyuracil 5'-diphenyl phosphate
-
pH 8.0, 25C
0.018
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
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
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
0.805
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2'-deoxyuracil
-
pH 8.0, 25C
0.298
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25C
0.547
5'-adamantoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25C, recombinant enzyme
0.35
5'-hexadecanoyl-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25C
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
-
-
2.5
5'-O-(4,4'-dimethoxytrityl)-2'-deoxyuridine
-
25C
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
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
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
0.00024
alpha,beta-imido-dUDP
-
25C
0.0039
alpha,beta-imido-dUTP
-
pH 7.5, 25C, wild-type enzyme
0.0009
alpha-beta-imido-dUTP
-
pH 8, 25C
0.5
Cu2+
-
-
0.0114
dUMP
-
pH 8.0, 25C, recombinant enzyme
0.0184
dUMP
-
-
0.099
dUMP
-
pH 7.0, 25C
0.115
dUTP
-
pH 7.0, 25C, recombinant enzyme
0.121
dUTP
-
pH 7.0, 25C, recombinant enzyme, without NaCl, presence of EDTA
0.092
dUTP-Co2+
-
pH 7.0, 25C, recombinant enzyme
0.0955
dUTP-Mg2+
-
pH 7.0, 25C, 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 37C
1
N-[3-(tert-butyl diphenyl silanyloxy)-propyl]-2-uracil acetamide
-
above
1
N-[4-(tert-butyl diphenyl silanyloxy)-butyl]-2-uracil acetamide
-
above
0.2271
2'-deoxy-5'-O-[tris(1-methylethoxy)silyl]uridine
-
pH 5.7-6.2, recombinant enzyme
additional information
2'-deoxy-5'-phenylmethylaminouracil
-
above 1 mM, pH 8.0, 25C
0.156
3-[5-(trityloxy)tetrahydrofuran-2-yl]pyridine-2,6(1H,3H)-dione
-
pH 8.0, 25C
additional information
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-2',3'-dideoxyuracil
-
above 1 mM, pH 8.0, 25C
0.807
5'-(2,2-dimethyl-1,1-diphenylpropan-1-yl)-3'-methyl-2',3'-dideoxyuracil
-
pH 8.0, 25C
additional information
5'-(2,3,3-trimethylbutan-2-yl)-3'-methyl-2',3'-dideoxyuracil
-
above 1 mM, pH 8.0, 25C
additional information
5'-(2,4-dimethyl-3-(1-methylethyl)pentan-3-yl)-2'-deoxyuracil
-
above 1 mM, pH 8.0, 25C
0.0718
dUTP-Mn2+
-
pH 7.0, 25C, recombinant enzyme
additional information
additional information
-
Ki of developed inhibitors higher than 1 mM
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.000033
(E)-3-(cyclopentyloxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.000028
(E)-3-(cyclopropylmethoxy)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.00034
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)-3-methoxybenzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.0016
(E)-N-(7-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-methylhept-5-en-2-yl)benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.01
(R)-1-(4-(2-(hydroxydiphenylmethyl)-pyrrolidin-1-yl)-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00041
(R)-N-(1-(3-(2,2-difluoroethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.00043
(R)-N-(1-(3-(cyclopentyloxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.00082
(R)-N-(1-(3-(cyclopropylmethoxy)phenyl)ethyl)-4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
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
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
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
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
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
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.001
1-(3-[[(2S)-2-[hydroxy[bis(2-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.001
1-(3-[[(2S)-2-[hydroxy[bis(3-methoxyphenyl)]methyl]pyrrolidin-1-yl]sulfonyl]propyl)pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00058
1-(4-[(2S)-2-[bis(3-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00035
1-(4-[(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.001
1-(4-[(2S)-2-[bis(4-chlorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0006
1-(4-[(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl)pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0073
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
1-[3-(4-benzylpiperidin-1-yl)-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0094
1-[3-([(2R)-2-[hydroxy(diphenyl)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00028
1-[3-([(2S)-2-[bis(3-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00031
1-[3-([(2S)-2-[bis(4-fluorophenyl)(hydroxy)methyl]pyrrolidin-1-yl]sulfonyl)propyl]pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.001
1-[3-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-3-oxopropyl]pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00015
1-[4-[(2S)-2-(diphenylmethyl)pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.001
1-[4-[(2S)-2-[bis[2-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.001
1-[4-[(2S)-2-[bis[3-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.001
1-[4-[(2S)-2-[bis[4-(benzyloxy)phenyl](hydroxy)methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.001 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00023
1-[4-[(2S)-2-[hydroxy[di(thiophen-3-yl)]methyl]pyrrolidin-1-yl]-4-oxobutyl]pyrimidine-2,4(1H,3H)-dione
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0042
1-[N-(2-triphenylmethylaminoethyl)-acetamide]uracil
-
-
0.0025
1-[N-(3-triphenylmethylaminopropyl)-acetamide]uracil
-
-
0.0029
1-[N-(4-triphenylmethylaminobutyl)-acetamide]uracil
-
above
0.0039
1-[N-(triphenylmethyl) diaminodi(n-propyl) acetamide]uracil
-
above
0.0045
1-[N-(triphenylmethylaminoethyl)-N-(aminoethyl) acetamide]uracil
-
above
0.083
1-[N-hydroxyethyl-N-(triphenylmethylamino) ethyl-acetamide]uracil
-
above
0.3
1-[[2-(trityloxy)ethoxy]methyl]pyrimidine-2,4(1H,3H)-dione
-
IC50 above 0.3 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0053
2',3',5'-trideoxy-3'-fluoro-5'-(tritylamino)uridine
-
activity against the parasites with IC50: 0.0053 mM
0.002
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
0.0045
2',5'-dideoxy-5'-(tritylamino)uridine
-
activity against the parasites with IC50: 0.0045 mM
0.0011
2'-deoxy-5'-O-(triphenylsilyl)uridine
-
activity against the parasites with IC50: 0.0011 mM
0.006
2'-deoxy-5'-O-trityluridine
-
activity against the parasites with IC50: 0.006 mM
0.013
2'-deoxy-5'-O-[tris(1-methylethoxy)silyl]uridine
-
activity against the parasites with IC50: 0.013 mM
0.015
2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.000073
3-(2,2-difluoroethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)propanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methylbutan-2-yl)propanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylethyl)propanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.022
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylhexan-3-yl)propanamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-phenylpropyl)propanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)propanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.000031
3-(cyclopentyloxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.000073
3-(cyclopropylmethoxy)-N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)phenyl)propan-2-yl)-benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.000035
3-(cyclopropylmethoxy)-N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0025
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methyl-1,1-diphenylpropan-2-yl)butanamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(1-hydroxy-2-methylpropan-2-yl)butanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0013
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)-N-methylbutanamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.016
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,2-diphenylethyl)butanamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2,4,4-trimethylpentan-2-yl)butanamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.0011
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-hydroxy-2,2-diphenylethyl)-N-methylbutanamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-1-phenylpropan-2-yl)butanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.021
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-methyl-4-phenylbutan-2-yl)butanamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(2-phenylpropan-2-yl)butanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(3-ethylpentan-3-yl)butanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-(diphenylmethyl)butanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-phenylbutanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
N,N-dibenzyl-3-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)propanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00127
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)-3-methoxybenzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.0018
N-(2-(4-((2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl)-phenyl)propan-2-yl)benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
-
0.03
N-benzyl-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)butanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.00004
N-[(1R)-1-[3-(cyclopropylmethoxy)phenyl]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 37C
0.074
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-D-alanyl-L-tyrosine
-
-
0.084
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-aspartic acid
-
-
0.081
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-glutamic acid
-
-
0.081
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-glutamine
-
-
0.081
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-lysine
-
-
0.087
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanyl-L-threonine
-
-
0.1
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-alanylglycine
-
-
0.084
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-lysine
-
-
0.091
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-threonine
-
-
0.076
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycyl-L-tyrosine
-
-
0.132
N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]glycylglycine
-
-
0.00034
N-[2-[3-(cyclopropylmethoxy)phenyl]propan-2-yl]-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 37C
0.0046
N-[3-(tert-butyl diphenyl silanyloxy)-propyl]-2-uracil acetamide
-
above
0.0037
N-[4-(tert-butyl diphenyl silanyloxy)-butyl]-2-uracil acetamide
-
above
0.0039
N-[5-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]-2-methylpentan-2-yl]benzenesulfonamide
-
in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
0.03
4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-N-[2-methyl-1-(naphthalen-2-yl)propan-2-yl]butanamide
-
IC50 above 0.03 mM, in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37C
additional information
additional information
-
IC50 values of the inhibitor cytotoxicity assay on rat LC6 cells, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0105
-
-
0.52
-
mutant enzyme E145Q, in 50 mM HEPES, pH 6.8, at 50C
1.33
-
mutant enzyme E145A, in 50 mM HEPES, pH 6.8, at 50C
1.46
-
enzyme from uninfected KB cells
2.171
-
enzyme from HSV-1-infected cells
8.8
-
wild type enzyme, in 50 mM HEPES, pH 6.8, at 50C
23.9
-
purified recombinant enzyme
25.75
-
purified recombinant enzyme
69
-
purified enzyme
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
P33316
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7 - 6.2
-
assay at
6 - 9
-
-
6.1 - 7.5
-
-
6.5 - 8.5
-
20 mM potassium phosphate buffer
7 - 8
-
-
7
-
broad plateau
7.4
-
assay at
7.4
-
assay at
7.5
-
assay at
7.5
-
assay at
7.6
-
assay at
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
50% of maximal activity at pH 6 and pH 10
6 - 7.5
-
pH 6.0: about 65% of maximal activity, pH 7.5: about 90% of maximal activity, about 5% of maximal activity at pH 5.0 and at pH 8.0
6 - 9
-
about 60% of maximal activity at pH 6.0 and at pH 9.0
6.5 - 8.5
-
enzyme from HSV-1 infected KB cells
6.5 - 8.5
-
-
7 - 10
-
strong increase of activity between pH 7 and 8
7 - 8
-
-
7 - 8
-
enzyme from uninfected KB cells
7.5 - 8.8
A7J1X3
pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
-
20
-
assay at
25
-
assay at
25
-
assay at
37
-
assay at
37
-
assay at
37
-
wild type enzyme
55
-
mutant enzyme E81S/T84R
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 60
-
very low activity above 60C
5 - 11
-
pH 5.0: about 65% of maximal activity, pH 11.0: about 90% of maximal activity
6.1 - 8
-
pH 5.0: no activity, pH 6.1-7.5: optimum, pH 8.0: about 60% of maximal activity
70 - 95
A7J1X3
temperature profile
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
calculated from amino acid sequence
6.5
-
sequence calculation
6.7
-
isoelectric focusing
9.1
Q6T180
calculated from sequence, pI: 9.07
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of patient with acute lymphocytic leukemia
Manually annotated by BRENDA team
-
an endocrine pancreatic cell line
Manually annotated by BRENDA team
-
dUTPase is upregulated in human tumor cells
Manually annotated by BRENDA team
-
primary cancer, patients after surgery, expression levels of the enzyme in the primary colorectal cancer of patients with and without distant metastases, the expression level is 3fold higher in the first case, overview
Manually annotated by BRENDA team
-
embryos respresenting the only step in the life cycle of Drosophila with clearly detectable levels of the enzyme
Manually annotated by BRENDA team
-
at the syncytial blastoderm stage, localization shifts of dUTPase isozymes within embryos, overview
Manually annotated by BRENDA team
-
amnion epithelial cells
Manually annotated by BRENDA team
-
enzyme form DUT-N is approximately 30fold more abundant in HeLa cells than in DUT-M cells
Manually annotated by BRENDA team
-
several astrocytoma, oligodendrogliomas, oligoastrocytomas, meningiomas, ependymomas, and metastatic acrcinomas, overview
Manually annotated by BRENDA team
-
KB cells induced or not induced with herpes simplex virus type 1
Manually annotated by BRENDA team
-
reduced enzyme expression
Manually annotated by BRENDA team
-
regenerating, activity in rat liver begins to rise 16 h after partial hepatectomy and reaches a maximum about 24 h after the operation, rising to at least 5 to 6 times the normal level
Manually annotated by BRENDA team
-
meristem cells, high levels of dUTPase in both resting and proliferating root meristem cells. Activity increase at the G1/S boundary, remains high throughout S phase, and shows almost undetectable levels during G1 and G2
Manually annotated by BRENDA team
-
activity in spleens of rats made anemic by phenylhydrazine is about 30times higher than that in spleens of untreated animals
Manually annotated by BRENDA team
-
proliferative intraerythroctic
Manually annotated by BRENDA team
additional information
-
intracellular labeling of the enzyme in intracranial tumors with marker Ki-67, overview
Manually annotated by BRENDA team
additional information
-
temporal expression pattern during the viral infection course, DUT is an early viral gene, overview
Manually annotated by BRENDA team
additional information
-
the enzyme is constitutively expressed in the adult fly
Manually annotated by BRENDA team
additional information
-
the enzyme is expressed in different life stages. Trypanosoma brucei brucei bloodstream form cell line S16 and the procyclic cell line 449
Manually annotated by BRENDA team
additional information
Trypanosoma brucei 427
-
the enzyme is expressed in different life stages. Trypanosoma brucei brucei bloodstream form cell line S16 and the procyclic cell line 449
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
one isozyme might be located in the cytoplasm
Manually annotated by BRENDA team
-
21 kDa isozyme, the 21 kDa isozyme is excluded from the nuclei during interphase, it is shifted to the nucleus during prophase and forthcoming mitotic steps
Manually annotated by BRENDA team
-
the short isoform of dUTPase (NTT-DUT) remains exclusively in the cytoplasm
Manually annotated by BRENDA team
Acholeplasma laidlawii B-PG9
-
-
-
Manually annotated by BRENDA team
-
enzyme form DUT-N
Manually annotated by BRENDA team
-
nuclear isozyme
Manually annotated by BRENDA team
-
one isozyme might be located in the nucleus
Manually annotated by BRENDA team
-
23 kDa isozyme, the 21 kDa isozyme is excluded from the nuclei during interphase, it is shifted to the nucleus during prophase and forthcoming mitotic steps
Manually annotated by BRENDA team
-
the long isoform of dUTPase (LD-DUT) is specifically targeted into the nucleus
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
-
-
Manually annotated by BRENDA team
-
enzyme form DUT-M
Manually annotated by BRENDA team
additional information
-
intracellular labeling of the enzyme in intracranial tumors with marker Ki-67, overview
-
Manually annotated by BRENDA team
additional information
-
subcellular localization study, no localization of the enzyme in mitochondria
-
Manually annotated by BRENDA team
additional information
-
analysis of subcellular localization of dUTPase, no localization in the mitochondrion or kinetoplast
-
Manually annotated by BRENDA team
additional information
-
both isoforms can be present within the nuclear microenvironment, although at different stages of cell cycle by strict timing to the nuclear cleavage phases
-
Manually annotated by BRENDA team
additional information
Trypanosoma brucei 427
-
analysis of subcellular localization of dUTPase, no localization in the mitochondrion or kinetoplast
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Epstein-Barr virus (strain B95-8)
Epstein-Barr virus (strain B95-8)
Epstein-Barr virus (strain B95-8)
Epstein-Barr virus (strain B95-8)
Epstein-Barr virus (strain B95-8)
Epstein-Barr virus (strain B95-8)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
-
low molecular weight enzyme form, gel filtration
209963
36000
-
gel filtration
209997
41000
-
gel filtration
209993
43000
-
gel filtration
209965
43000
A7J1X3
recombinant enzyme, gel filtration
688794
45000
-
gel filtration, density gradient centrifugation in presence of MgCl2
209972
45000
-
gel filtration
209987
46000
-
enzyme from uninfected KB cells, gel filtration
209974
46000
-
gel filtration, glycerol density gradient sedimentation
209977
48000
-
high molecular weight enzyme form, gel filtration
209963
48000
-
gel filtration
209973
48000
-
recombinant enzyme, gel filtration
670775
53000
-
enzyme from HSV-1 infected KB cells, gel filtration
209974
54000
-
truncated enzyme, gel filtration
656212
54000
-
recombinant His-tagged enzyme, native PAGE
670091
56600
P33317
gel filtration
718787
58500
-
sucrose density gradient centrifugation
209980
60000
-
gel filtration
209968, 209980
62440
-
gel filtration
655557
62850
-
gel filtration
209985
63000
-
N-terminally truncated short isoform NTT-DUT
711982
64000
-
gel filtration
209979
64000
-
SDS-PAGE of cross-linked subunits
655557
64500
-
gel filtration, sucrose density gradient centrifugation
209964
65000
-
full length enzyme, gel filtration
656212
68000
-
gel filtration
209969
69000
-
long isoform LD-DUT
711982
70000
-
about, gel filtration
670999
136000
Q57872
gel filtration
648212
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 16600, calculation from nucleotide sequence
?
P9WNS5
x * 25000, recombinant enzyme, SDS-PAGE
?
-
x * 174000, about, amino acid sequence calculation
?
-
x * 21000, isozyme 1, SDS-PAGE, x * 23000, isozyme 2, SDS-PAGE
?
Q6T180
x * 22043, His6-tagged enzyme, calculated from sequence
?
-
x * 25000, recombinant enzyme, SDS-PAGE
-
?
Pyrococcus woesei DSM 3773
-
x * 22043, His6-tagged enzyme, calculated from sequence
-
dimer
-
2 * 22500, SDS-PAGE
dimer
-
2 * 31420, calculation from amino acid sequence
dimer
-
1 * 45000-50000, SDS-PAGE
dimer
-
crystal structure analysis
dimer
-
2 * 30300, calculated from amino acid sequence
dimer
-
2 * 32000, SDS-PAGE, 2 * 32065, calculated from amino acid sequence
dimer
-
two identical subunits, crystal structure analysis
dimer
-
2 * 30300, recombinant enzyme, SDS-PAGE
dimer
-
cyrstal structure analysis, overview
dimer
A7J1X3
2 * 17700, about, sequence calculation
dimer
-
hinge prolines play a role in oligomer assembly
dimer
Trypanosoma brucei 427
-
-
-
hexamer
-
composed of two identical trimers, crystal structure analysis
hexamer
Q57872
two trimers assemble into a hexamer, crystal structure analysis
homotrimer
-
-
homotrimer
-
-
homotrimer
-
-
homotrimer
-
3 * 16100, SDS-PAGE
homotrimer
-
folding pattern and active site architecture, overview
homotrimer
-
with interfaces formed between subunit surfaces, in the central channel, and by C-terminal beta-strand swapping. Analysis of intersubunit interactions reveals an important cohesive role for the C-terminus
homotrimer
P33317
3 * 18100, His tagged enzyme, calculated from amino acid sequence
monomer
P03195
-
monomer
-
1 * 35000, virally induced enzyme, SDS-PAGE
monomer
-
overall enzyme fold, the enzyme contains five characteristic sequence motifs and one active site, three-domain structural organization and secondary structure, overview
tetramer
-
4 * 16000, SDS-PAGE
tetramer
Escherichia coli overproducing
-
4 * 16000, SDS-PAGE
-
trimer
-
each subunit contains an active site
trimer
-
crystal structure
trimer
-
3 * 14300, ion spray mass spectroscopy
trimer
-
3 * 16000, SDS-PAGE
trimer
-
3 * 16400, calculation from amino acid sequence
trimer
-
3 * 19500, SDS-PAGE
trimer
-
3 * 19800, full length enzyme, 3 * 17200, truncated enzyme, mass spectrometry, gel filtration
trimer
-
3 * 16000, recombinant enzyme, SDS-PAGE
trimer
-
3 * 176000, recombinant His-tagged enzyme, SDS-PAGE
trimer
-
3 * 23000, recombinant enzyme, SDS-PAGE
trimer
-
each subunit contains an active site, alpha,beta-imino-dUTP which induces an allosteric conformational change within the central threefold channel of the homotrimer
trimer
-
homotrimer, crystal structure
trimer
-
homotrimer
-
monomer
-
structure modeling, secondary structure analysis
additional information
-
molecular structure modeling
additional information
-
the enzyme contains five conserved N-terminal domains
additional information
-
the enzyme interacts with several protein partners in the cell
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
nuclear dUTPase is phosphorylated by the phosphorylated cyclin-cdc2 complex
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, 25C, 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
Q9STG6
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, 17C, 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
-
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, 4C, X-ray diffraction structure determination and analysis at 1.88 A resolution
-
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, 20C, 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
-
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)
P03195
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
Q57872
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
-
purified recombinant bifunctional dCTP deaminase:dUTPase in complex with inhibitor thymidine triphosphate, hanging drop vapor diffusion method, 15C, 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
P9WNS5
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
P33317
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
-
enzyme in complex with inhibitor dUDP, crystal structure determination and analysis
-
vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
stable for several h
209998
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 55
-
stable against denaturation
657286
27 - 41
-
20 min, stable
209965
37
-
5 min, stable
209997
42
-
t1/2: 18 min, in presence of 2 mM 2-mercaptoethaol
209978
45
-
t1/2: 22 min for enzyme from uninfected KB cells
209974
45
-
t1/2: 35 min for enzyme from HSV-1 infected KB cells
209974
45
-
5 min, 28% loss of activity
209997
53
-
melting point, increases in the presence of Mg2+ and substrate
655586
54
-
melting point
656212
55
-
1 h, stable
209973
55
-
5 min, complete inactivation
209997
61.7
-
melting temperature
686744
74.5
-
melting point
655586
95
A7J1X3
purified recombinant enzyme, half-life is 170 min
688794
additional information
-
4 mM Mg2+ stabilizes at 37C
209965
additional information
-
heat-induced denaturation, unfolding is irreversible in all samples
697957
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dUMP protects against tryptic digestion, slight fragmentation caused by frequent freezing and thawing that does not affect the activity
-
stable to freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable for at least 3 months
-
-70C, stable for at least 5 months
-
0C, stable for at least 3 months
-
-20C, 7 days, 70% loss of activity of uninduced dUTPase
-
-20C, 7 days, 2% loss of activity of HSV-1 induced dUTPase
-
-70C, 50 mM HEPES, pH 7.2, 150 mM NaCl, 2 mM dithiothreitol
Q57872
-20C, stable for several months
-
-80C, stable for 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from to homogeneity
Q9STG6
recombinant enzyme of Bacillus subtilis temperate bacteriophage SPbeta from Escherichia coli strain BL21(DE3) by phosphocellulose chromatography to homogeneity
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and gel filtration
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by hydroxyapatite chromatography, and two steps of anion exchange chromatography
-
recombinant protein
-
recombinant enzyme
-
recombinant protein
-
subcellular fractionation
-
phosphocellulose column chromatography
-
large-scale
-
phosphocellulose column chromatography
-
recombinant proteins
-
partial
-
phosphocellulose column chromatography
-
recombinant enzyme by ion exchange chromatography and gel filtration
-
recombinant enzyme from Escherichia coli by phosphocellulose chromatography and gel filtration to near homogeneity
-
recombinant N-terminally His-tagged wild-type dUTPase and mutant F158W by nickel affinity chromatography
-
native enzyme from virus
-
Ni-NTA column chromatography
P03195
recombinant His-tagged enzyme from Escherichia coli by metal affinity chromatography, cleavage of the tag
-
recombinant enzyme from Escherichia coli strain BL21 by hydroxyapatite and anion exchange chromatography
-
recombinant C-terminal domain nucleocapsid fusion protein or free enzyme from Escherichia coli by heparin affinity chromatography and gel filtration
-
recombinant protein
Q57872
Ni-NTA column chromatography
A0QW08
Ni-NTA column chromatography
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by streptomycin precipitation, anion exchange chromatography, dialysis, and ammonium sulfate fractionation to homogeneity
P9WNS5
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant protein using His-tag
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
phosphocellulose column chromatography
-
phosphocellulose column chromatography and Superdex 200 gel filtration
-
recombinant enzyme by gel filtration
-
recombinant enzyme from Escherichia coli by phosphocellulose chromatography and gel filtration to near homogeneity
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by cation exchange chromatography, gel filtration, and anion exchange chromatography to near homogeneity
-
nickel affinity resin column chromatography and Superdex-200 gel filtration
P33317
recombinant wild-type and mutant enzymes from yeast strains
P33317
recombinant N-terminally His6-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli by cobalt chelating affinity chromatography and gel filtration
A7J1X3
recombinant enzyme
-
recombinant protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme expression
Q9STG6
gene yosS encoded by the Bacillus subtilis temperate bacteriophage SPbeta, DNA and amino acid sequence determination and analysis, functional overexpression in Escherichia coli strain BL21(DE3)
-
genes yncF and yosS, DNA and amino acid sequence determination and analysis, high level overexpression of N-terminally His6-tagged enzymes in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3)
-
overexpression in Escherichia coli strain BL21(DE3)
-
expressed in different Escherichia coli strains
-
expression in Schneider 2 cells
-
expression of the core enzyme lacking the 28-residue-long C-terminal fly-specific segment
-
two isozymes, DNA and amino acid sequence determination and analysis, developmental expression analysis, overview
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
two naturally occuring variants of the enzyme are expressed as recombinant proteins in Escherichia coli
-
cloning of the dut gene in the runaway-replication plasmid pKN402A and in the lambdapL-promoter plasmid pHUB2
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
native and mutant enzyme
-
recombinant expression
-
overexpression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression in Escherichia coli
-
expression of N-terminally His-tagged wild-type dUTPase and mutant F158W
-
expression of the His-tagged nuclear isoform and its F158W mutant
-
isolation of cDNA clones and characterization
-
recombinant expression
-
expressed in Escherichia coli BL21(DE3) cells
P03195
expressed in HeLa cells, in KB cells, or in RAJI cells
-
gene BLLF3, overexpression of His-tagged enzyme in Escherichia coli
-
expressed in Escherichia coli
-
overexpression in Escherichia coli strain BL21
-
expression as C-terminal domain fusion protein with the nucleocapsid protein in Escherichia coli
-
expressed in Escherichia coli BL21
Q57872
enzyme expression in Escherichia coli strain BL21(DE3)
P9WNS5
expressed in Escherichia coli BL21(DE3) (pLysS) cells
-
expressed in Escherichia coli BL21-Gold (DE3) as His-tag fusion protein
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
DNA and amino acid sequence determination and analysis, the gene locates on chromosome 11, overexpression in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression of the recombinant enzyme
-
the expression of N-terminal His(6)-tagged Pwo dUTPase is performed in Escherichia coli BL21(DE3)pLysS and Eschwerichia coli Rosetta(DE3)pLysS strain that contains plasmid encoding additional copies of rare Escherichia coli tRNAs. Escherichia coli Rosetta(pLysS) strain is found with two times higher expression yield of His(6)-tagged Pwo dUTPase than Escherichia coli BL21(DE3)pLysS. The His(6)-tagged Pwo dUTPase is purified on Ni(2+)-IDA-Sepharose, dialyzed, and the enzyme activity is investigated. THe His(6)-tag domain has no influence on dUTP hydrolytic activity. dUTP is generated during PCR from dCTP, which inhibits the polymerization of DNA catalyzed by DNA polymerase with 3'-5' exonuclease activity
Q6T180
gene DUT, DNA and amino acid sequence determination and analysis, phylogenetic analysis, temporal expression pattern during the viral infection course, overexpression as EGFP-fusion enzyme in the cytoplasm of EPC cells, no effects on virus replication by enzyme overexpression, overview
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21-Gold(DE3) cells
P33317
gene DUT1, DNA and amino acid sequence determination and analysis of DUT1 alleles, genotyping, expression of wild-type and mutant enzymes in yeast strains
P33317
gene wdut, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
gene dut, DNA and amino acid sequence determination and analysis, high level overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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expression in Escherichia coli
O71028
DNA and amino acid sequence determination and analysis, His-tagged enzyme expression in Escherichia coli
A7J1X3
gene DUT, recombinant expression
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expressed in Escherichia coli BL21(DE3)
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expressed in Escherichia coli strain BW286
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DURP gene of herpesvirinae, localization in the genome and organization, overview
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expression in Escherichia coli under the control of a bacteriophage T7 promoter
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E81S/T84R
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the mutations lead to an increase in the optimal temperature of the enzyme to 55C
E81S/T84R
Chlorella virus IL-3A
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the mutations lead to an increase in the optimal temperature of the enzyme to 55C
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D90N
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site-directed mutagenesis
S72A
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site-directed mutagenesis, steady-state kinetic characterization, S72A mutation causes a 725fold reduction in kcat and a 35fold reduction in KM.
D49N/F158W
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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
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the mutant shows severely decreased catalytic activity compared to the wild type enzyme
F158W
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site-directed mutagenesis, inactive mutant
F158W
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the mutant shows decreased catalytic activity compared to the wild type enzyme
C4S
P03195
the mutant shows increased activity compared to the wild type enzyme
D131E
P03195
the mutant is completely devoid of enzymatic activity
D131N
P03195
the mutant shows decreased activity compared to the wild type enzyme
D131S
P03195
the mutant shows decreased activity compared to the wild type enzyme
D131S/G78D
P03195
the mutant shows decreased activity compared to the wild type enzyme
F273A
P03195
the deletion of the flexible C-terminal tail carrying motif V results in a protein completely devoid of enzymatic activity
R268A
P03195
the mutant shows decreased activity compared to the wild type enzyme
E145A
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the mutant shows reduced specific activity towards dUTP
E145Q
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the mutant shows reduced specific activity towards dUTP
D28N/H145W
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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
H145A
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the mutant shows decreased catalytic activity compared to the wild type enzyme
H145W
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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
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the mutant shows decreased catalytic activity compared to the wild type enzyme
D28N/H145W
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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
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H145A
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the mutant shows decreased catalytic activity compared to the wild type enzyme
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F46A
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the mutation does not affect the nucleotide hydrolase activity of dUTPase
I117A
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the mutation does not affect the nucleotide hydrolase activity of dUTPase
K96A
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the mutation does not affect the nucleotide hydrolase activity of dUTPase
D32A
P33317
the mutant exhibits negligible activity
D85A
P33317
the mutant exhibits negligible activity
D87A
P33317
the mutant exhibits negligible activity
D87A/R137A/D85A
P33317
inactive
F142A
P33317
the mutant exhibits very low activity
G82S
P33317
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
P33317
the mutant shows essentially the wild type affinity for dUTP and greatly reduced activity
R111A
P33317
the mutant has reduced activity and lower substrate affinity (increased Km) compared to the wild type enzyme
R137A
P33317
the mutant exhibits negligible activity
R68A
P33317
the mutant exhibits very low activity
S69A
P33317
the mutant exhibits negligible activity
DELTA160-187
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truncated form
additional information
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removal of the physiologically present, very flexible 28-residue C-terminal segment does not perturb catalytic function but facilitates crystallization
D90N
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no effect on Km, strong decrease in catalytic activity, H-bonding significantly altered
additional information
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mutations of a suggested hinge proline destabilize Escherichia coli dUTPase without preventing trimeric organization
F158W
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the mutation has no significant effect on the catalytic properties of dUTPase
additional information
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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
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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
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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
H145W
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the mutation has no significant effect on the catalytic properties of dUTPase
additional information
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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
H145W
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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, the mutation has no significant effect on the catalytic properties of dUTPase, the mutant shows decreased catalytic activity compared to the wild type enzyme
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additional information
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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
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Y88A
P33317
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
additional information
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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
Trypanosoma brucei 427
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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the enzyme is a target for drugs against campylobacteriosis
medicine
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potential drug target
drug development
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inhibitor development against the enzyme can be useful in antiviral and anticancer therapy
pharmacology
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the enzyme is a chemotherapeutic target
drug development
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inhibitor development against the enzyme can be useful in antiviral and anticancer therapy
drug development
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the enzyme is a target for development of antimicrobial agents
pharmacology
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the enzyme is a chemotherapeutic target
synthesis
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can reduce uracil incorporation into DNA
diagnostics
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the enzyme can be a biomarker for exposure to N-methyl-N'-nitro-N-nitrosoguanidine exposure since the compound leads to release of the enzyme, besides other proteins, to the extracellular compartment from amnion epithelial cells, overview
drug development
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the enzyme is a potential antiparasitic drug target
drug development
P33316
the enzyme might be a target for drug development
drug development
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the nuclear isoform of the enzyme is a target for anticancer chemotherapeutic strategies
drug development
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dUTPase family of enzymes are promising targets for anticancer and antimicrobial therapies
drug development
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the enzyme is a target for development of therapeutic drugs against EBV infection
pharmacology
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the enzyme is a potential target for antiviral drug design
drug development
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the enzyme is a potential antiparasitic drug target
medicine
A0QW08
dUTPase is a target for antitubercular drugs
medicine
Mycobacterium smegmatis mc2155
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dUTPase is a target for antitubercular drugs
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drug development
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dUTPase is a promising antituberculotic drug target
medicine
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potential target for anti-tuberculosis therapy
medicine
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dUTPase is a target for antitubercular drugs
drug development
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dUTPase is a promising antituberculotic drug target
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medicine
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potential target for anti-tuberculosis therapy, dUTPase is a target for antitubercular drugs
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drug development
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dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors
drug development
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the enzyme is a potential antiparasitic drug target
drug development
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the enzyme is a potential drug target against malaria
drug development
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the enzyme is a target for anti-malarial drugs
drug development
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induced fit drug design
medicine
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potential target for treatment of Chagas' disease