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2-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
2-thio-5'-UMP + diphosphate
-
substrate is anti-thyroid drug
-
?
4-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
4-thio-UMP + diphosphate
-
-
-
-
?
4-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
4-thiouridine monophosphate + diphosphate
-
-
-
?
5-bromo-UMP + diphosphate
5-bromouracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
5-chloro-UMP + diphosphate
5-chlorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
5-fluoro-UMP + diphosphate
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
5-iodo-UMP + diphosphate
5-iodouracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
uridine + ATP
UMP + ADP
the bifunctional enzyme UK/UPRT also performs the uridine kinase reaction, EC 2.7.1.48
-
-
?
additional information
?
-
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
recombinant bifunctional enzyme UK/UPRT
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
1.6fold higher specific activity compared to uracil
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
-
r
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
216% of the activity with uracil
-
-
r
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
recombinant fusion enzyme in RM1 tumors of lung, spleen, heart, and prostate
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
recombinant fusion enzyme
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
no activity
-
-
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
97% of the activity with uracil
-
-
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
97% of the activity with uracil
-
-
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
no activity
-
-
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
no activity
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
maximum activity is obtained with 0.4-0.5 mM uracil in the presence of 1 mM PRPP, decreasing with increasing uracil concentrations thereafter. The activity in the presence of 0.5 mM uracil and at varying concentrations of PRPP is maximal at 0.75-1.0 mM PRPP, remaining constant thereafter
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
maximum activity is obtained with 0.4-0.5 mM uracil in the presence of 1 mM PRPP, decreasing with increasing uracil concentrations thereafter. The activity in the presence of 0.5 mM uracil and at varying concentrations of PRPP is maximal at 0.75-1.0 mM PRPP, remaining constant thereafter
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
maximum activity is obtained with 0.4-0.5 mM uracil in the presence of 1 mM PRPP, decreasing with increasing uracil concentrations thereafter. The activity in the presence of 0.5 mM uracil and at varying concentrations of PRPP is maximal at 0.75-1.0 mM PRPP, remaining constant thereafter
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
maximum activity is obtained with 0.4-0.5 mM uracil in the presence of 1 mM PRPP, decreasing with increasing uracil concentrations thereafter. The activity in the presence of 0.5 mM uracil and at varying concentrations of PRPP is maximal at 0.75-1.0 mM PRPP, remaining constant thereafter
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
maximum activity is obtained with 0.4-0.5 mM uracil in the presence of 1 mM PRPP, decreasing with increasing uracil concentrations thereafter. The activity in the presence of 0.5 mM uracil and at varying concentrations of PRPP is maximal at 0.75-1.0 mM PRPP, remaining constant thereafter
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
incorporation of uracil into nucleotides
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
equilibrium lies far in the direction of UMP formation
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
highly specific for uracil
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
equilibrium lies far in the direction of UMP formation
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
5-phospho-alpha-D-ribose 1-diphosphate binding site
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
5-phospho-alpha-D-ribose 1-diphosphate binding site
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
highly specific for uracil and analogues
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
highly specific for uracil and analogues
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
the enzyme is involved in the uracil salvage pathway, UPRT is a major cell supplier of UMP synthesized from uracil provided by preformed nucleic acid degradation, uracil salvage and pyrimidine biosynthetic pathways, overview
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
the enzyme is involved in the uracil salvage pathway, UPRT is a major cell supplier of UMP synthesized from uracil provided by preformed nucleic acid degradation, uracil salvage and pyrimidine biosynthetic pathways, overview
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Lactobacillus bifidus
-
-
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
the enzyme is specific for uracil
-
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
the enzyme is specific for uracil
-
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
highly specific for uracil
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
highly specific for uracil
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
transfer to N1 of uracil
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate binding site
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
highly specific for uracil
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
-
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate binding site
-
?
additional information
?
-
-
no catalysis of exchange reaction between uracil-UMP and diphosphate-5-phospho-alpha-D-ribose 1-diphosphate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no substrates: thymine, hypoxanthine
-
-
?
additional information
?
-
-
no substrates: cytosine, orotic acid
-
-
?
additional information
?
-
-
no substrates: thymine, hypoxanthine
-
-
?
additional information
?
-
-
no substrates: cytosine, orotic acid
-
-
?
additional information
?
-
Lactobacillus bifidus
-
orotic acid is no substrate
-
-
?
additional information
?
-
-
no substrates: cytosine, orotic acid
-
-
?
additional information
?
-
-
no substrates: cytosine, orotic acid
-
-
?
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metabolism
the enzyme is involved in the metabolism of uracil and related compounds in plants catalyzing the uracil salvage, which is of major importance for plant development, overview
evolution
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human
evolution
-
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human
-
evolution
-
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human
-
evolution
-
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human
-
evolution
-
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human
-
malfunction
gene upp disruption does not affect Mycobacterium tuberculosis growth in Middlebrook 7H9 medium, and it is not required for Mycobacterium tuberculosis virulence in a mouse model of infection
malfunction
the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. The mutant's growth can be restored by uridine. In silico analysis of the AgUPRT does not highlight any particular feature that can account for limitations in its enzymatic activity
malfunction
-
the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. The mutant's growth can be restored by uridine. In silico analysis of the AgUPRT does not highlight any particular feature that can account for limitations in its enzymatic activity
-
malfunction
-
the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. The mutant's growth can be restored by uridine. In silico analysis of the AgUPRT does not highlight any particular feature that can account for limitations in its enzymatic activity
-
malfunction
-
gene upp disruption does not affect Mycobacterium tuberculosis growth in Middlebrook 7H9 medium, and it is not required for Mycobacterium tuberculosis virulence in a mouse model of infection
-
malfunction
-
gene upp disruption does not affect Mycobacterium tuberculosis growth in Middlebrook 7H9 medium, and it is not required for Mycobacterium tuberculosis virulence in a mouse model of infection
-
malfunction
-
the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. The mutant's growth can be restored by uridine. In silico analysis of the AgUPRT does not highlight any particular feature that can account for limitations in its enzymatic activity
-
malfunction
-
the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. The mutant's growth can be restored by uridine. In silico analysis of the AgUPRT does not highlight any particular feature that can account for limitations in its enzymatic activity
-
physiological function
UPRTs, on-essential, energy-saving enzymes, are involved in the salvage of pyrimidines by catalyzing the formation of uridine monophosphate from uracil and phosphoribosylpyrophosphate. Uracil salvage is of major importance for plant development, especially early development
physiological function
uracil phosphoribosyltransferase (UPRT) catalyzes the reversible transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl1-diphosphate (PRPP) to uracil N1 to form uridine-5'-monophosphate, UMP, in the presence of Mg2+. Nucleosides are essential metabolites in numerous biochemical processes in all living organisms
physiological function
uracil phosphoribosyltransferase (UPRT) is the pyrimidine salvage pathway enzyme responsible for converting uracil to uridine monophosphate in the presence of phosphoribosyl pyrophosphate (PRPP). Uracil-mediated regulation mechanism of the UPRT activity
physiological function
uracil phosphoribosyltransferase from Mycobacterium tuberculosis (MtUPRT) converts uracil and 5-phosphoribosyl-alpha-1-diphosphate into diphosphate and uridine 5'-monophosphate, the precursor of all pyrimidine nucleotides. Although MtUPRT is a key enzyme of the pyrimidine salvage pathway, as it directly synthetizes UMP from uracil, its levels remain constant under hypoxic conditions. Accordingly, MtUPRT does not appear to play a significant role in the non-replicating latent stage of Mycobacterium tuberculosis in vitro. In addition, the upp gene is not required for the full virulence of Mycobacterium tuberculosis in mice in the model tested. In conclusion, MtUPRT is unlikely to be a good target for anti-tuberculosis drug development
physiological function
-
uracil phosphoribosyltransferase (UPRT) is the pyrimidine salvage pathway enzyme responsible for converting uracil to uridine monophosphate in the presence of phosphoribosyl pyrophosphate (PRPP). Uracil-mediated regulation mechanism of the UPRT activity
-
physiological function
-
uracil phosphoribosyltransferase (UPRT) is the pyrimidine salvage pathway enzyme responsible for converting uracil to uridine monophosphate in the presence of phosphoribosyl pyrophosphate (PRPP). Uracil-mediated regulation mechanism of the UPRT activity
-
physiological function
-
uracil phosphoribosyltransferase from Mycobacterium tuberculosis (MtUPRT) converts uracil and 5-phosphoribosyl-alpha-1-diphosphate into diphosphate and uridine 5'-monophosphate, the precursor of all pyrimidine nucleotides. Although MtUPRT is a key enzyme of the pyrimidine salvage pathway, as it directly synthetizes UMP from uracil, its levels remain constant under hypoxic conditions. Accordingly, MtUPRT does not appear to play a significant role in the non-replicating latent stage of Mycobacterium tuberculosis in vitro. In addition, the upp gene is not required for the full virulence of Mycobacterium tuberculosis in mice in the model tested. In conclusion, MtUPRT is unlikely to be a good target for anti-tuberculosis drug development
-
physiological function
-
uracil phosphoribosyltransferase from Mycobacterium tuberculosis (MtUPRT) converts uracil and 5-phosphoribosyl-alpha-1-diphosphate into diphosphate and uridine 5'-monophosphate, the precursor of all pyrimidine nucleotides. Although MtUPRT is a key enzyme of the pyrimidine salvage pathway, as it directly synthetizes UMP from uracil, its levels remain constant under hypoxic conditions. Accordingly, MtUPRT does not appear to play a significant role in the non-replicating latent stage of Mycobacterium tuberculosis in vitro. In addition, the upp gene is not required for the full virulence of Mycobacterium tuberculosis in mice in the model tested. In conclusion, MtUPRT is unlikely to be a good target for anti-tuberculosis drug development
-
physiological function
-
uracil phosphoribosyltransferase (UPRT) is the pyrimidine salvage pathway enzyme responsible for converting uracil to uridine monophosphate in the presence of phosphoribosyl pyrophosphate (PRPP). Uracil-mediated regulation mechanism of the UPRT activity
-
physiological function
-
uracil phosphoribosyltransferase (UPRT) is the pyrimidine salvage pathway enzyme responsible for converting uracil to uridine monophosphate in the presence of phosphoribosyl pyrophosphate (PRPP). Uracil-mediated regulation mechanism of the UPRT activity
-
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P131D
-
site-directed mutagenesis, 2-step mutagenic PCR, exchange of proline in 5-phosphoribose 1-diphosphate binding site, 50-60fold reduction of catalytic rate in both reaction directions, about 100fold increase in KM for uracil, strongly reduced Km for 5-phosphoribose 1-diphosphate
C128V
site-directed mutagenesis, required for structural sudy
K150A
site-directed mutagenesis, slightly reduced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy
K59A
site-directed mutagenesis, slightly enhanced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy
R68A
site-directed mutagenesis, slightly reduced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy
additional information
construction of T-DNA insertion enzyme mutants, inability to salvage uracil caused a lightdependent dramatic pale-green to albino phenotype, dwarfism and the inability to produce viable progeny in loss-of-function mutants, plastid biogenesis and starch accumulation are affected in all tissues, with the exception of stomata, phenotypes, overview. A graduation in the tolerance to 5-fluorouracil is observed among the upp(+/) heterozygous plants. Functional complementation of the enzyme-deficient Escherichia coli mutant strain BM604, overview. No significant decrease in UPRT activity is measured in the mutants disrupted at uracil kinase-like proteins UKL loci
additional information
the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. Uridine is the only intermediate of the pyrimidine salvage pathway able to fully restore this mutant's growth. Overexpression of the AgUPRT encoding-gene in Ashbya gossypii mutant Agura3 leads to similar growth on rich medium containing 5 mM uracil or uridine
additional information
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the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. Uridine is the only intermediate of the pyrimidine salvage pathway able to fully restore this mutant's growth. Overexpression of the AgUPRT encoding-gene in Ashbya gossypii mutant Agura3 leads to similar growth on rich medium containing 5 mM uracil or uridine
additional information
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the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. Uridine is the only intermediate of the pyrimidine salvage pathway able to fully restore this mutant's growth. Overexpression of the AgUPRT encoding-gene in Ashbya gossypii mutant Agura3 leads to similar growth on rich medium containing 5 mM uracil or uridine
-
additional information
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the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. Uridine is the only intermediate of the pyrimidine salvage pathway able to fully restore this mutant's growth. Overexpression of the AgUPRT encoding-gene in Ashbya gossypii mutant Agura3 leads to similar growth on rich medium containing 5 mM uracil or uridine
-
additional information
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the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. Uridine is the only intermediate of the pyrimidine salvage pathway able to fully restore this mutant's growth. Overexpression of the AgUPRT encoding-gene in Ashbya gossypii mutant Agura3 leads to similar growth on rich medium containing 5 mM uracil or uridine
-
additional information
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the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. Uridine is the only intermediate of the pyrimidine salvage pathway able to fully restore this mutant's growth. Overexpression of the AgUPRT encoding-gene in Ashbya gossypii mutant Agura3 leads to similar growth on rich medium containing 5 mM uracil or uridine
-
additional information
engineering the yeast fluorocytosine deaminase (FCY1) gene by creating a fusion with the bacterial uracil phosphoribosyl transferase (UPP) gene results in a recombinant protein that converts the precursor 5-fluorocytosine (5-FC) into 5-fluorouracyl, a drug used in the treatment of a range of cancers, which triggers DNA and RNA damage. The FCY-UPP gene construct is expressed in specific cell types using enhancer trap lines and promoters, demonstrating that this marker acts in a cell-autonomous manner. It can inactivate slow developmental processes like lateral root formation by targeting pericycle cells. A role for the lateral root cap and the epidermis in controlling root growth, a faster response, is also revealed. The 5-FC precursor acts systemically, as demonstrated by its ability to inhibit stomatal movements when supplied to the roots in combination with a guard cell-specific promoter. The tissular inactivation is reversible, and can therefore be used to synchronize plant responses or to determine cell type-specific functions during different developmental stages
additional information
seven independent upp mutants are constructed and found to excrete low amounts of pyrimidines to the growth medium, pyrimidine-dependent transcription regulation of the biosynthetic pyrimidine pyrR1-B-C-Aa1-Ab1-D-F-E operon is impaired in the upp mutants, overview, model of pyrP pyrimidine-dependent regulation by transcription attenuation
additional information
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seven independent upp mutants are constructed and found to excrete low amounts of pyrimidines to the growth medium, pyrimidine-dependent transcription regulation of the biosynthetic pyrimidine pyrR1-B-C-Aa1-Ab1-D-F-E operon is impaired in the upp mutants, overview, model of pyrP pyrimidine-dependent regulation by transcription attenuation
additional information
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seven independent upp mutants are constructed and found to excrete low amounts of pyrimidines to the growth medium, pyrimidine-dependent transcription regulation of the biosynthetic pyrimidine pyrR1-B-C-Aa1-Ab1-D-F-E operon is impaired in the upp mutants, overview, model of pyrP pyrimidine-dependent regulation by transcription attenuation
-
additional information
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expression of fusion protein cytosine deaminase combined with uracil phosphoribosyl transferase leads to local and distant bystander effects against intraprostatic mouse androgen-refractory prostate, RM1, tumors in immunocompetent mice, CDUPRT-GDEPT expression significantly suppresses the aggressive growth of RM1 prostate tumors and lung pseudo-metastases via immune mechanisms involving necrosis and apoptosis, overview
additional information
generation of an upp knockout strain by allelic replacement (using the pPR27xylE plasmid, which contains a thermosensitive origin of replication, the xylE reporter gene and the sacB counterselectable marker), evaluation of it in infected mice. Knockout and complemented strains are validated by a functional assay of uracil incorporation. Recombinant expression of Mycobacterium smegmatis gene upp in Mycobacterium tuberculosis wild-type strain H37Rv, resulting in strain CP, and in the upp knockout (KO) variant of H37Rv. Swiss male mice are infected intravenously with 5 × 105 colony forming units (CFU) of Mycobacterium tuberculosis H37Rv wild-type, knockout, or CP strains
additional information
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generation of an upp knockout strain by allelic replacement (using the pPR27xylE plasmid, which contains a thermosensitive origin of replication, the xylE reporter gene and the sacB counterselectable marker), evaluation of it in infected mice. Knockout and complemented strains are validated by a functional assay of uracil incorporation. Recombinant expression of Mycobacterium smegmatis gene upp in Mycobacterium tuberculosis wild-type strain H37Rv, resulting in strain CP, and in the upp knockout (KO) variant of H37Rv. Swiss male mice are infected intravenously with 5 × 105 colony forming units (CFU) of Mycobacterium tuberculosis H37Rv wild-type, knockout, or CP strains
additional information
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generation of an upp knockout strain by allelic replacement (using the pPR27xylE plasmid, which contains a thermosensitive origin of replication, the xylE reporter gene and the sacB counterselectable marker), evaluation of it in infected mice. Knockout and complemented strains are validated by a functional assay of uracil incorporation. Recombinant expression of Mycobacterium smegmatis gene upp in Mycobacterium tuberculosis wild-type strain H37Rv, resulting in strain CP, and in the upp knockout (KO) variant of H37Rv. Swiss male mice are infected intravenously with 5 × 105 colony forming units (CFU) of Mycobacterium tuberculosis H37Rv wild-type, knockout, or CP strains
-
additional information
-
generation of an upp knockout strain by allelic replacement (using the pPR27xylE plasmid, which contains a thermosensitive origin of replication, the xylE reporter gene and the sacB counterselectable marker), evaluation of it in infected mice. Knockout and complemented strains are validated by a functional assay of uracil incorporation. Recombinant expression of Mycobacterium smegmatis gene upp in Mycobacterium tuberculosis wild-type strain H37Rv, resulting in strain CP, and in the upp knockout (KO) variant of H37Rv. Swiss male mice are infected intravenously with 5 × 105 colony forming units (CFU) of Mycobacterium tuberculosis H37Rv wild-type, knockout, or CP strains
-
additional information
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sensitivity of cells to 5-FU can be further increased by expression of UPRT, useful in an approach for the management of graft-versus-host disease occurring after allogeneic hematopoietic cell transplantation by genetical engineering of donor T lymphocytes to express a suicide gene, i.e. the Herpes simplex virus thymidine kinase HSV-tk gene, to facilitate negative selection, combination of UPRT expression with expression of cytosine deaminase, an alternative gene for negative selection, converting 5-fluorocytosine to the toxic metabolite 5-fluorouracil, a construct NG/CDiU expressing UPRT and NG/CD, using a bicistronic message, provides the greatest UPRT activity and killing, overview
additional information
covalent immobilization of uracil phosphoribosyltransferase (UPRT) from Thermus thermophilus HB8 onto glutaraldehyde-activated magnetic iron oxide porous microparticles (MTtUPRT). The support is activated by contacting the microspheres with 0.2 ml of 50 mM sodium phosphate buffer, pH 8.5, containing 5% w/v glutaraldehyde during 3 h at 25°C, and then washed thoroughly with distilled water to remove the excess activating agent. Finally, activated microspheres are washed and equilibrated in binding buffer (50 mM potassium phosphate buffer, pH 8.5), shortly prior to use. According to the catalyst load experiments, MTtUPRT3 is selected as optimal biocatalyst. MTtUPRT3 is active and stable in a broad range of temperature (70-100°C) and in the pH interval 6.0-8.0, displaying maximum activity at 100°C and pH 7.0 (activity 968 IU/g support, retaining activity 100%). In addition, MTtUPRT3 can be reused up to 10 times in the synthesis of uridine-5'-monophosphate (UMP), completely stable for 6 cycles. Biocatalyst recycling is studied by employing MTtUPRT3 in consecutive reactions. MTtUPRT3 is successfully applied in the sustainable synthesis of different 5-modified uridine-5'-monophosphates at short times
additional information
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covalent immobilization of uracil phosphoribosyltransferase (UPRT) from Thermus thermophilus HB8 onto glutaraldehyde-activated magnetic iron oxide porous microparticles (MTtUPRT). The support is activated by contacting the microspheres with 0.2 ml of 50 mM sodium phosphate buffer, pH 8.5, containing 5% w/v glutaraldehyde during 3 h at 25°C, and then washed thoroughly with distilled water to remove the excess activating agent. Finally, activated microspheres are washed and equilibrated in binding buffer (50 mM potassium phosphate buffer, pH 8.5), shortly prior to use. According to the catalyst load experiments, MTtUPRT3 is selected as optimal biocatalyst. MTtUPRT3 is active and stable in a broad range of temperature (70-100°C) and in the pH interval 6.0-8.0, displaying maximum activity at 100°C and pH 7.0 (activity 968 IU/g support, retaining activity 100%). In addition, MTtUPRT3 can be reused up to 10 times in the synthesis of uridine-5'-monophosphate (UMP), completely stable for 6 cycles. Biocatalyst recycling is studied by employing MTtUPRT3 in consecutive reactions. MTtUPRT3 is successfully applied in the sustainable synthesis of different 5-modified uridine-5'-monophosphates at short times
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cloning from a fetal brain cDNA library, DNA and amino acid sequence determination, subcloning in Escherichia coli strain DH5alpha, expression of His6-tagged enzyme in Escherichia coli strain M15, phylogenetic analysis, expressionin AD293 cells, tissue and subcellular expression pattern
co-expression of gene CodA, encoding cytosine deaminase, and gene upp, encoding uracil phosphoribosyl transferase, renders HeLa cells sensitive to 5-fluorocytosine, converted to toxic 5-fluorouracil by cytosine deaminase, and enhanced a bystander effect mediated by a gap junction mechanism, 1% cytosine deaminase+-UPP+ cells are able to kill 40% of the cell population if the cells are communicating
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coexpression of the uracil phosphoribosyltransferase gene with a chimeric human nerve growth factor receptor/yeast cytosine deaminase fusion gene, using a single retroviral vector, augments cytotoxicity of transduced human T cells, CEM cells, exposed to 5-fluorocytosine
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cytosine deaminase-UPRT-red fluorescence protein fusion proteins are expressed in Rattus norvegicus R-3327-AT cells
DNA and amino acid sequence determination and analysis of the natural chimeric gene UK/UPRT1 encoding uridine kinase, UK, and uracil phosphoribosyltransferase, UPRT, expressionin Escherichia coli, transient expression as C-terminally GFP-tagged enzyme in Arabidopsis thaliana mesophyll protoplasts, 5-FU sensitivity of the Escherichia coli upp mutants is influenced by the expression of AtUK/UPRT1, as well as the 5-FU and 5-FD sensitivity of Escherichia coli upp-udk mutants, overview
DNA and amino acid sequence determination and analysis, overexpression in enzyme-deficient Escherichia coli
DNA sequence determination and analysis, gene upp belongs to purMN operon, complementation of deficient Escherichia coli strain
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DNA sequence determination, functional overexpression in Escherichia coli BL21(DE3)plyS
expressed in A2780 cells, A2780/Taxol cells, Skov3 cells, and Skov3/Taxol cells
expressed in AsPC-1, BxPC3, CaPan-1, MIA, PaCa-2, Panc-1, and HT-29 cell lines
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expressed in BHK-21 cells and HAT-29 cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21Star (DE3) One Shot cells
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expressed in Escherichia coli strain JM109
expressed in Escherichia coli strain M15 and in AD-293 cells
expressed in Escherichia coli Tuner (DE3) cells
expressed in HaP-T1 cells
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expressed in HeLa cells
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expressed in LNCaP cells
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expression in Escherichia coli
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expression in human adipose tissue-derived mesenchymal stem cells
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expression of the fusion gene CDUPRT, combining cytosine deaminase combined with uracil phosphoribosyl transferase, in RM1 cancer cells in a gene therapeutic approach, overview
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functional overexpression in Escherichia coli JM109
gene AGOS_AFR052C, sequence comparisons, phylogenetic tree, functional recombinant expression of the enzyme with an N-terminal fusion to TrxA as a soluble enzyme in Escherichia coli
gene UPP, DNA and amino acid sequence determination and analysis, gene structure, sequence comparison, and phylogenetic analysis, Comparison to uracil kinase-like proteins possessing UPRT domains. The single nuclear gene encoding UPP targeted to plastids is responsible for almost all UPRT activity in Arabidopsis thaliana
gene upp, recombinant expression, the basal level of MtUPRT expression is independent of either growth medium used, addition of bases, or oxygen presence/absence
gene upp, recombinant overexpression of 35S:FCY-UPP and pMYB60:FCY-UPP constructs in Arabdopsis thaliana ecotype Col-0, which affects the effect of 5-fluorouracil (5-FC) on the plants compared to wild-type plants, analysis of the tissue specificity of the FCY-UPP tandem, overview. The enzyme tandem is expressed in the xylem pole pericycle cells from which lateral roots are being formed. Expressing FCYUPP in the lateral root cap and epidermis using the J0951 enhancer trap line results in a strong reduction of primary root growth. Similarly, when FCY-UPP proteins are expressed in the guard cells using the pMYB60 promoter, no reduction in total leaf area is observed. These observations suggest that both the FCY-UPP tandem protein and the products of 5-FC incorporation remain in the cells where the construct is expressed, at least on a short time-scale. A tagged version of FCY-UPP fused to the GFP reporter is expressed under the epidermis-specific promoter of WEREWOLF
gene upp, upp gene is part of the lp_2376-glyA-upp operon, upp expression depends on the upp-pyrP gene cluster, pyrP encodes a high affinity uracil transporter, which is expressed and regulated independently of upp, overview
overexpressing from plasmid in Escherichia coli strain NF1815
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overexpression of wild-type and mutant P131D in Escherichia coli
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recombinant expression of N-terminal His6-tagged TtUPRT
wild-type and mutant C128V
DNA and amino acid sequence determination and analysis, overexpression in enzyme-deficient Escherichia coli
DNA and amino acid sequence determination and analysis, overexpression in enzyme-deficient Escherichia coli
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functional overexpression in Escherichia coli JM109
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functional overexpression in Escherichia coli JM109
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Escherichia coli, Lactobacillus bifidus, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus 09X
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577-582
2015
Mycobacterium tuberculosis (P9WFF3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WFF3)
brenda
Narayanan, S.; Sanpui, P.; Sahoo, L.; Ghosh, S.S.
Unravelling the potential of a new uracil phosphoribosyltransferase (UPRT) from Arabidopsis thaliana in sensitizing HeLa cells towards 5-fluorouracil
Int. J. Biol. Macromol.
91
310-316
2016
Arabidopsis thaliana
brenda
Hasegawa, N.; Abei, M.; Yokoyama, K.K.; Fukuda, K.; Seo, E.; Kawashima, R.; Nakano, Y.; Yamada, T.; Nakade, K.; Hamada, H.; Obata, Y.; Hyodo, I.
Cyclophosphamide enhances antitumor efficacy of oncolytic adenovirus expressing uracil phosphoribosyltransferase (UPRT) in immunocompetent Syrian hamsters
Int. J. Cancer
133
1479-1488
2013
Syrian hamster adenovirus
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Soysa, R.; Wilson, Z.N.; Elferich, J.; Forquer, I.; Shinde, U.; Riscoe, M.K.; Yates, P.A.; Ullman, B.
Substrate inhibition of uracil phosphoribosyltransferase by uracil can account for the uracil growth sensitivity of Leishmania donovani pyrimidine auxotrophs
J. Biol. Chem.
288
29954-29964
2013
Leishmania donovani
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Villela, A.D.; Ducati, R.G.; Rosado, L.A.; Bloch, C.J.; Prates, M.V.; Goncalves, D.C.; Ramos, C.H.; Basso, L.A.; Santos, D.S.
Biochemical characterization of uracil phosphoribosyltransferase from Mycobacterium tuberculosis
PLoS ONE
8
e56445
2013
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Leonhardt, N.; Divol, F.; Chiarenza, S.; Deschamps, S.; Renaud, J.; Giacalone, C.; Laurent, N.; Berthome, R.; Peret, B.
Tissue-specific inactivation by cytosine deaminase/uracil phosphoribosyl transferase as a tool to study plant biology
Plant J.
101
731-741
2019
Escherichia coli (P0A8F0)
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Del Arco, J.; Galindo, J.; Clemente-Suarez, V.J.; Corrales, A.; Fernandez-Lucas, J.
Sustainable synthesis of uridine-5-monophosphate analogues by immobilized uracil phosphoribosyltransferase from Thermus thermophilus
Biochim. Biophys. Acta
1868
140251
2020
Thermus thermophilus (Q5SIQ7), Thermus thermophilus
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Villela, A.D.; Pham, H.; Jones, V.; Grzegorzewicz, A.E.; Rodrigues-Junior, V.D.; Campos, M.M.; Basso, L.A.; Jackson, M.; Santos, D.S.
Analysis of uracil phosphoribosyltransferase expression in Mycobacterium tuberculosis and evaluation of upp knockout strain in infected mice
FEMS Microbiol. Lett.
364
gnx023
2017
Mycobacterium tuberculosis (P9WFF3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WFF3), Mycobacterium tuberculosis ATCC 25618 (P9WFF3)
brenda
Silva, R.; Aguiar, T.Q.; Oliveira, C.; Domingues, L.
Physiological characterization of a pyrimidine auxotroph exposes link between uracil phosphoribosyltransferase regulation and riboflavin production in Ashbya gossypii
New Biotechnol.
50
1-8
2019
Eremothecium gossypii (Q754M0), Eremothecium gossypii, Eremothecium gossypii CBS 109.51 (Q754M0), Eremothecium gossypii FGSC 9923 (Q754M0), Eremothecium gossypii ATCC 10895 (Q754M0), Eremothecium gossypii NRRL Y-1056 (Q754M0)
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