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Information on EC 2.4.2.9 - uracil phosphoribosyltransferase
for references in articles please use BRENDA:EC2.4.2.9
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.2 Pentosyltransferases
2.4.2.9 uracil phosphoribosyltransferase
The enzyme appears in viruses and cellular organisms
- 2.4.2.9
- 5-fluorouracil
- pyrimidine
-
salvage
- 5-fluorocytosine
-
suicide
-
prodrug
- orotate
-
bystander
- 5-fluorouridine
-
oncolytic
-
markerless
-
phosphoribosyltransferases
-
counterselectable
-
flucytosine
- 4-thiouracil
- medicine
-
virotherapy
-
cd/5-fc
-
gene-directed
- synthesis
- analysis
- molecular biology
- pharmacology
showSynonyms
uracil phosphoribosyltransferase, uprt, uprtase, uracil phosphoribosyl transferase, cd-uprt, ump pyrophosphorylase, cytosine deaminase/uracil phosphoribosyltransferase, mtuprt, cytosine deaminase-uracil phosphoribosyltransferase, uridine monophosphate pyrophosphorylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AFR052C
AFR052Cp
AGOS_AFR052C
AgUPRT
cytosine deaminase/uracil phosphoribosyltransferase
-
bifunctional fusion enzyme
MtUPRT
phosphoribosyltransferase, uracil
-
-
-
-
Rv3309c
UMP pyrophosphorylase
-
-
-
-
UMP:pyrophosphate phosphoribosyltransferase
-
-
-
-
UPP
UPRT
UPRTase
uracil phosphoribosyl transferase
uridine 5'-phosphate pyrophosphorylase
-
-
-
-
uridine kinase/uracil phosphoribosyltransferase 1
the enzyme contains a uridine domain and the C-terminal region consists of a UPRT domain
uridine monophosphate pyrophosphorylase
-
-
-
-
uridylate pyrophosphorylase
-
-
-
-
uridylic pyrophosphorylase
-
-
-
-
additional information
UPRT
-
-
-
-
UPRTase
-
-
-
-
additional information
-
PyrR protein is a bifunctional protein, that primarily regulates the expression of pyrimidine biosynthetic pyr genes, but also catalyses the uracil phosphoribosyltransferase reaction, little amino acid sequence similarities to other bacterial UPRTases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
modelling of enzyme-5-phospho-alpha-D-ribose 1-diphosphate complex
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
sequential reaction mechanism
-
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
sequential reaction mechanism
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
ping-pong reaction mechanism
-
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Pro131 is of little importance for 5-phospho-alpha-D-ribose 1-diphosphate binding, but critical for binding of uracil to the enzyme-5-phospho-alpha-D-ribose 1-diphosphate complex
-
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
ping pong steady state kinetic pattern, ordered bi-bi mechanism, model, no formation of the phosphoribosyl-enzyme intermediate predicted by classic ping pong kinetics
-
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
active sites pointing away from each other, a long arm from each monomer subunit wraps around the other subunit
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
rapid-random equilibrium mechanism
-
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
rapid-random equilibrium mechanism
Giardia duodenalis Portland
-
-
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
pyrimidine nucleobases salvage I
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SYSTEMATIC NAME
IUBMB Comments
UMP:diphosphate phospho-alpha-D-ribosyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9030-24-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
2-thio-5'-UMP + diphosphate
-
Substrates: substrate is anti-thyroid drug
Products: -
Products: -
?
4-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
4-thio-UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
4-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
4-thiouridine monophosphate + diphosphate
Substrates: -
Products: -
Products: -
?
5-bromo-UMP + diphosphate
5-bromouracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
5-chloro-UMP + diphosphate
5-chlorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
5-chlorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-chloro-UMP + diphosphate
Substrates: -
Products: -
Products: -
?
5-fluoro-UMP + diphosphate
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
5-hxdroxymethyluracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-hydroxymethyl-UMP + diphosphate
Substrates: -
Products: -
Products: -
?
5-iodo-UMP + diphosphate
5-iodouracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
5-iodouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-iodo-UMP + diphosphate
Substrates: -
Products: -
Products: -
?
trifluorothymine + 5-phospho-alpha-D-ribose 1-diphosphate
?
Substrates: -
Products: -
Products: -
?
uridine + ATP
UMP + ADP
Substrates: the bifunctional enzyme UK/UPRT also performs the uridine kinase reaction, EC 2.7.1.48
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
Substrates: recombinant bifunctional enzyme UK/UPRT
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
Substrates: -
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: 1.6fold higher specific activity compared to uracil
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: -
Products: -
Products: -
r
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: 216% of the activity with uracil
Products: -
Products: -
r
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: 216% of the activity with uracil
Products: -
Products: -
r
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
Substrates: -
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: recombinant fusion enzyme in RM1 tumors of lung, spleen, heart, and prostate
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: recombinant fusion enzyme
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
Syrian hamster adenovirus
-
Substrates: -
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: no activity
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
Substrates: -
Products: -
Products: -
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
Substrates: 97% of the activity with uracil
Products: -
Products: -
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
Substrates: 97% of the activity with uracil
Products: -
Products: -
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
Substrates: no activity
Products: -
Products: -
?
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
-
Substrates: no activity
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: 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
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: 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
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii CBS 109.51
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii CBS 109.51
Substrates: 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
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii FGSC 9923
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii FGSC 9923
Substrates: 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
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii NRRL Y-1056
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii NRRL Y-1056
Substrates: 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
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: incorporation of uracil into nucleotides
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: equilibrium lies far in the direction of UMP formation
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: highly specific for uracil
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: equilibrium lies far in the direction of UMP formation
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: 5-phospho-alpha-D-ribose 1-diphosphate binding site
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: highly specific for uracil and analogues
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: highly specific for uracil and analogues
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Giardia duodenalis Portland
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: 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
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: 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
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Lactobacillus bifidus
-
Substrates: -
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: the enzyme is specific for uracil
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: the enzyme is specific for uracil
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Syrian hamster adenovirus
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: highly specific for uracil
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: highly specific for uracil
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: transfer to N1 of uracil
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: 5-phospho-alpha-D-ribose 1-diphosphate binding site
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: highly specific for uracil
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: 5-phospho-alpha-D-ribose 1-diphosphate binding site
Products: -
Products: -
?
additional information
?
-
-
Substrates: no catalysis of exchange reaction between uracil-UMP and diphosphate-5-phospho-alpha-D-ribose 1-diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: thymine, hypoxanthine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: cytosine, orotic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: thymine, hypoxanthine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: cytosine, orotic acid
Products: -
Products: -
?
additional information
?
-
Lactobacillus bifidus
-
Substrates: orotic acid is no substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: cytosine, orotic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: cytosine, orotic acid
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with thymine
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
uridine + ATP
UMP + ADP
Substrates: the bifunctional enzyme UK/UPRT also performs the uridine kinase reaction, EC 2.7.1.48
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
Substrates: recombinant bifunctional enzyme UK/UPRT
Products: -
Products: -
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
-
Substrates: recombinant fusion enzyme in RM1 tumors of lung, spleen, heart, and prostate
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii CBS 109.51
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii FGSC 9923
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Eremothecium gossypii NRRL Y-1056
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
UMP + diphosphate
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: incorporation of uracil into nucleotides
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: 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
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: 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
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: the enzyme is specific for uracil
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: the enzyme is specific for uracil
Products: -
Products: -
r
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Syrian hamster adenovirus
-
Substrates: -
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
-
Substrates: pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: pyrimidine salvage enzyme, no de novo synthesis of pyrmidines
Products: -
Products: -
?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
divalent cations
Mg2+
Mn2+
Zn2+
additional information
Co2+
-
UPRTase can use Mn2+, Co2+ and Zn2+ instead of Mg2+. While the saturation curve for Mg2+ is smoothly increasing, these three metal ions are inhibitory at higher concentrations
divalent cations
-
preference of activation by divalent cations in decreasing order: Mn2+, Co2+, Cd2+, Mg2+, Ni2+, Ca2+, all 1 mM
Mn2+
-
can partly substitute for Mg2+ at 5 mM, less effective, inhibitory at higher concentration
Mn2+
-
UPRTase can use Mn2+, Co2+ and Zn2+ instead of Mg2+. While the saturation curve for Mg2+ is smoothly increasing, these three metal ions are inhibitory at higher concentrations
Zn2+
-
can partly substitute for Mg2+ at 5 mM, less effective, inhibitory at higher concentration
Zn2+
-
UPRTase can use Mn2+, Co2+ and Zn2+ instead of Mg2+. While the saturation curve for Mg2+ is smoothly increasing, these three metal ions are inhibitory at higher concentrations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CTP
-
powerful inhibitor in combination with UMP. CTP and UMP can be bound simultaneously
CTP
inhibitory allosteric regulation by CTP. The regulatory triphosphate binds at a site in the center of the tetramer changing the quaternary arrangement. The effector contacts Pro94 at the beginning of a long beta-strand in the dimer interface, which extends into a flexible loop over the active site, two flexible loops. In the inhibited state, residues, Tyr123 and Lys125 contribute to the configuration of the active site for UMP rather than PRPP binding. The C-terminal Gly216 participates in a hydrogen-bond network in the dimer interface that stabilizes the inhibited, but not the activated, state
diphosphate
-
noncompetitive against uracil, competitive against 5-phosphoribose 1-diphosphate
UMP
-
powerful inhibitor in combination with CTP. CTP and UMP can be bound simultaneously
additional information
-
not significantly activated or inhibited by ATP, UTP, and CTP
-
additional information
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
-
additional information
-
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
-
additional information
-
the enzyme undergoes a transition from a weakly active or inactive T-state, favored by binding of UMP and CTP, to an active R-state, favored by binding of GTP and 5-phosphoribosyl 1-diphosphate
-
additional information
-
no inhibition by cytosine, orotic acid, 6-azauracil
-
additional information
-
no inhibition by thymine, cytosine, orotic acid, and hypoxanthine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alendronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.5fold, increases the initial rate of synthesis of UMP 2.3fold
clodronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2fold, increases the initial rate of synthesis of UMP 1.9fold
etidronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.8fold, increases the initial rate of synthesis of UMP 2.1fold
glutathione
Lactobacillus bifidus
-
omission of glutathione reduces the reaction rate about 25%
pamidronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.6fold, increases the initial rate of synthesis of UMP 2.1fold
GTP
-
highly activating at low 5-phosphoribose 1-diphosphate concentration, e.g. 0.2 mM, by modification of the structure from dimer/trimer to pentamer/hexamer
GTP
-
about 5-7fold increase of Km for 5-phosphoribose 1-diphosphate, unaltered Vmax
GTP
-
effect is pH-dependent, pH 7.5: lowers Km value for 5-phospho-alpha-D-ribose 1-diphosphate and increases Vmax 2fold, no effect on Km for uracil, pH 8.0: no effect
GTP
-
strong activation at pH 6 and at pH 8. The concentration of GTP required for half-maximal activation is about 0.080 mM
GTP
-
strong stimulation, binds cooperatively with 5-phosphoribosyl 1-diphosphate
GTP
activating allosteric regulation by GTP. The regulatory triphosphate binds at a site in the center of the tetramer changing the quaternary arrangement. The effector contacts Pro94 at the beginning of a long beta-strand in the dimer interface, which extends into a flexible loop over the active site. In the GTP-bound state, two flexible loop residues, Tyr123 and Lys125, bind the diphosphate moiety of PRPP in the neighboring subunit and contribute to catalysis. The C-terminal Gly216 participates in a hydrogen-bond network in the dimer interface that stabilizes the inhibited, but not the activated, state
GTP
activation, stabilization of the tetrameric structure at 2 mM, without GTP enzyme forms dimers
GTP
about 5-7fold increase of Km for 5-phosphoribose 1-diphosphate, unaltered Vmax
additional information
-
the enzyme undergoes a transition from a weakly active or inactive T-state, favored by binding of UMP and CTP, to an active R-state, favored by binding of GTP and 5-phosphoribosyl 1-diphosphate
-
additional information
-
no activating effect with methylene biphosphonate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
5-phospho-alpha-D-ribose 1-diphosphate
recombinant wild-type, with GTP
0.049
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 8.0, presence of 1 mM GTP
0.0993
5-phospho-alpha-D-ribose 1-diphosphate
-
with uracil as cosubstrate, at pH 7.5 and 25°C
0.115
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 6.1, presence of 1 mM GTP
0.216
5-phospho-alpha-D-ribose 1-diphosphate
recombinant wild-type, without GTP
additional information
additional information
-
Km-value for 5-phosphoribose 1-diphosphate of the mutant P131D is very low and difficult to determine
-
additional information
additional information
Km-values, recombinant mutant enzymes
-
additional information
additional information
-
Km-values, recombinant mutant enzymes
-
additional information
additional information
allosteric transition, structural and kinetic studies, overview
-
additional information
additional information
-
allosteric transition, structural and kinetic studies, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.1
5-phospho-alpha-D-ribose 1-diphosphate
-
activated by 1 mM GTP
additional information
additional information
recombinant wild-type and mutant enzymes
-
additional information
additional information
-
recombinant wild-type and mutant enzymes
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
product inhibition pattern
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
over 60% of maximal activity within this range, profile overview
5.5 - 8
-
pH 3.8: no activity, pH 5.5: optimum, pH 8: about 20% of maximal activity
5.8 - 7
-
pH 5.8: about 55% of maximal activity, pH 7.0: about 45% of maximal activity
7.2 - 8
-
pH 7.2: about 50% of activity maximum, pH 8.0: about 70% of activity maximum
7.5 - 8.5
-
more than 90% activity between 7.5 and 8.5 with sharp drops in activity 0.5 pH units outside this range
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 100
over 40% of maximal activity within this range, profile overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.85
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
AtUK/UPRT1; ecotype Col-0, several strains, natural chimeric gene AtUK/UPRT1 encoding uridine kinase, UK, and uracil phosphoribosyltransferase, UPRT
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
quantitative analysis of the tissue expression pattern
brenda
additional information
quantitative analysis of the tissue expression pattern
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
physiological function
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
Eremothecium gossypii CBS 109.51
-
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human
-
evolution
Eremothecium gossypii FGSC 9923
-
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human
-
evolution
Eremothecium gossypii NRRL Y-1056
-
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
-
plants lacking this enzyme are strongly compromised in chloroplast function. Reduced enzyme contents provoke severely impaired plant growth and development
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
Eremothecium gossypii CBS 109.51
-
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
Eremothecium gossypii FGSC 9923
-
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
Eremothecium gossypii NRRL Y-1056
-
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 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
-
the enzyme is required to establish a functional cytochrome b6f complex. The enzyme assists in stabilization Rieske iron sulfur protein PetC during import, processing or targeting to the thylakoid membrane, or protects it against proteolytic degradation
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
Eremothecium gossypii CBS 109.51
-
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
Eremothecium gossypii FGSC 9923
-
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
Eremothecium gossypii NRRL Y-1056
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
111000
-
sucrose density gradient centrifugation and gel filtration in presence of substrates
22500
24000 - 27600
-
recombinant enzyme, gel filtration and DNA sequence determination
27000
36000
63000
-
sucrose density gradient centrifugation and gel filtration in absence of substrates
80000
additional information
-
gel filtration and sedimentation analyses: a smaller oligomeric, less active form, dimeric or trimeric, predominates in absence of substrates, a larger aggregated, more active form, pentameric or hexameric, predominates in presence of substrates
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
trimer
additional information
additional information
the recombinant chimeric enzyme UK/UPRT1 shows an N-terminal region containing a UK domain and the C-terminal region consisting of an UPRT domain
additional information
-
the recombinant chimeric enzyme UK/UPRT1 shows an N-terminal region containing a UK domain and the C-terminal region consisting of an UPRT domain
additional information
a tetramer of 2 dimers, equilibrium between dimeric and tetrameric form
additional information
-
a tetramer of 2 dimers, equilibrium between dimeric and tetrameric form
additional information
2 conserved sequences: Asp131-Ser139 contains the 5-phosphoribose 1-diphosphate binding motif and binds the ribose 5'-phosphate part of UMP, Tyr193-Ala201 is specific for uracil phosphoribosyltransferases and binds the uracil part of UMP
additional information
-
2 conserved sequences: Asp131-Ser139 contains the 5-phosphoribose 1-diphosphate binding motif and binds the ribose 5'-phosphate part of UMP, Tyr193-Ala201 is specific for uracil phosphoribosyltransferases and binds the uracil part of UMP
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
computational docking of inhibitor 5-fluorouracil to the active site of the enzyme. 5-fluorouracil forms hydrogen bonds with residues Tyr192, Gly196, and Leu197 in the complex. 5-fluorouracil shows low average free energy binding with the enzyme which indicates stronger binding than the natural substrate uracil
-
sitting drop vapor diffusion method, using 0.1 M sodium acetate trihydrate pH 4.6, 1.5 M sodium formate with a 2:1 reservoir-to-protein solution ratio at 25°C
enzyme in complex with UMP, enzyme in complex with CTP, structure with UMP bound in half of the active sites. Hanging-drop vapour-diffusion method
two structures of the activated state enzyme in complex with GTP, X-ray diffraction structure determination and analysis at 2.8 A resolution, the first structure which contains PRPP in all active sites, and 2.9 A resolution, for the second structure with PRPP in two sites and the hydrolysis products ribose-5-phosphate and diphosphate in the other sites, respectively, and a third structure of the enzyme in complex with UMP and the allosteric inhibitor CTP
hanging drop-vapour diffusion method, enzyme complexed with uracil and 5-phosphoribose 1-diphosphate, 20 mg/ml, mixing of equal volumes, 15 mM sodium citrate/phosphate, 0.2 M NaCl, pH 4.7, 10% polyethylene glycol 3400, X-ray diffraction structure analysis, dynamic light scattering
hanging drop-vapour diffusion technique, 2.0 M ammonium phosphate as precipitant, pH 8.0, room temperature, X-ray diffraction structure analysis, crystals are enzymatically active, wild-type and mutant enzymes
vapour diffusion using hanging or sitting drops, room temperature, protein solution 20 mg/ml, pH 7.0, 5 mM phosphate, 0.003 ml + 0.003 ml reservoir solution, pH 7.5, 6-10% polyethylene glycol 4000, 0.1 M HEPES, crystals appeared after 3 weeks, structure determination and analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
A168G/Y228A
the mutant shows increased activity compared to the wild type enzyme
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
M166A/A168G/Y228A
the mutant shows increased activity compared to the wild type enzyme
R68A
site-directed mutagenesis, slightly reduced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy
additional information
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
-
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
-
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
Eremothecium gossypii CBS 109.51
-
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
Eremothecium gossypii FGSC 9923
-
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
Eremothecium gossypii NRRL Y-1056
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
56 - 57
-
10 min, 50% loss of activity, recombinant wild-type and mutant, scanning calorimetry
60
80
60
-
2 min, complete loss of activity, 1 mM uracil + 0.1 EDTA protect partially
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against buffers of low ionic strength invariably results in complete inactivation, whereas after 3 h dialysis against 0.5 M KCl only 40% of the activity is lost
Lactobacillus bifidus
-
enzyme is highly unstable, dimethyl sulfoxide stabilizes during purification
-
ethylene glycol, significantly increases stability with virtually no loss of activity after storage at 4°C for 13 days or after 1 year at -70°C
-
GTP, 5 mM with 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 2 mM 2-mercaptoethanol, labilizes with only 15% activity remaining after 13 days, labilizing effect abolished in presence of 5-phospho-alpha-D-ribose 1-diphosphate
-
immobilization of mutant enzyme A168G/Y228A onto Ni2+ chelate leads to 92% retained activity and 3-5fold enhanced stability at 50-60°C compared to the wild type enzyme, as well as 80% retained activity after 7 cycles (5 min) in 5-fluoro-UMP synthesis. Immobilization of mutant enzyme A168G/Y228A onto glutaraldehyde-activated microparticles leads to 27% retained activity and 8-20fold enhanced stability at 50-60°C compared to the wild type enzyme, as well as 70% retained activity after 10 cycles (20 min) in 5-fluoro-UMP synthesis.
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, partially purified enzyme, loss of 10% activity within 2 weeks
Lactobacillus bifidus
-
0°C, enzyme concentration 0.001 mg/ml, 50% loss of activity in 1 h
4°C for 13 days or 1 year at -70°C, ethylene glycol, significantly increases stability with virtually no loss of activity
-
4°C, 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 2 mM 2-mercaptoethanol, 44% loss of activity after 8 d
-
4°C, concentrated enzyme is stable for several months, on dilution occurs rapid loss of activity
4°C, purified detagged recombinant enzyme, in Tris-NaCl buffer, stable for at least 1 week
4°C, Tris-HCl, pH 8.0, 1 mM EDTA, 2 mM DTT, 1 mM UMP, loss of 40% activity in 1 week
-
4°C, Tris-HCl, pH 8.0, 1 mM EDTA, 2 mM DTT, loss of 70% activity in 4 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-300 gel filtration
-
MonoQ column chromatography and Superdex 200 gel filtration
only partial, due to the labile nature of the enzyme further purification is unsuccessful
-
partial
recombinant enzyme from Escherichia coli, cleavage of the TrxA fusion protein with TEV protease
recombinant from Escherichia coli
recombinant His6-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography
recombinant wild-type and mutant P131D from overexpressing Escherichia coli
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
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
-
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
-
expression of the fusion gene CDUPRT, combining cytosine deaminase combined with uracil phosphoribosyl transferase, in RM1 cancer cells in a gene therapeutic approach, overview
-
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
His6-tagged wild type and mutant enzymes A168G/Y228A and M166A/A168G/Y228A are expressed in Escherichia coli BL21(DE3) cells as His6-tagged enzyme
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
biosynthetic labeling of RNA with uracil phosphoribosyltransferase allows cell-specific microarray analysis of mRNA synthesis and decay
medicine
molecular biology
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 tissue-specific FCY-UPP system is a great tool to inactivate cells in a precise spatial and temporal manner, method evaluation, overview
pharmacology
potential target for the development of new antibiotics
synthesis
MtTtUPRT is successfully applied in the enzymatic synthesis of therapeutic NMP analogues. The immobilized enzyme is usable as a biocatalyst in the synthesis of different 5-modified uridine-5'-monophosphates at short times. MTtUPRT3 can be reused up to 8 times in the synthesis of uridine-5'-monophosphate (UMP) with maximum activity at 100°C and pH 7.0 (activity 968 IU/g support, retaining activity 100%). Potential application of MTtUPRT3 as industrial biocatalyst
additional information
medicine
increased expression of UPRT may improve the antitumoral effect of 5-fluorouracil and 5-fluorocytosine, and thereby enhance the potential gene-directed enzyme prodrug therapy
medicine
-
combination of 5-flurocytosine/cytosine deaminase-uracil phosphoribosyltransferase with curcumin can be a potential chemosensitization strategy for cancer treatment
medicine
-
the CD/UPRT construct confers 5-fluorocytosine sensitivity to some pancreatic cell lines
medicine
-
the efficiacy of 5-fluorouracil-based chemotherapy in prostate cancers can be significantly improved by targeted expression of the suicide gene UPRT under the control of the human prostate-specific membrane antigen promotor/enhancer
medicine
-
in presence of 5-fluorocytosine, rat glioblastoma cells C6 and C6r5-FU are sensitive to the cytotoxic effect of human adipose tissue-derived mesenchymal stem cells expressing yeast cytosinedeaminase::uracil phosphoribosyltransferase. The stem cells migrate to glioblastoma cells in vivo and mediate inhibition of glioblastoma growth
medicine
-
the enzyme augments the cancer treatment efficacy of 5-fluorouracil in vitro
medicine
Syrian hamster adenovirus
-
the enzyme increases the sensitivity to 5-fluorouracil in HaP-T1 cells in vitro
additional information
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
additional information
-
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
additional information
-
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
-
additional information
-
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flaks, J.G.
Nucleotide synthesis from 5-phosphoribosylpyrophosphate
Methods Enzymol.
6
136-158
1963
Lactobacillus bifidus, Escherichia coli, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus 09X
-
brenda
Asai, T.; Lee, C.S.; Chandler, A.; O'Sullivan, W.J.
Purification and characterization of uracil phosphoribosyltransferase from Crithidia luciliae
Comp. Biochem. Physiol. B
95
159-163
1990
Crithidia luciliae
-
brenda
Plunkett, W.; Moner, J.G.
UMP pyrophosphorylase of Tetrahymena pyriformis. Partial purification and properties
Arch. Biochem. Biophys.
187
264-271
1978
Tetrahymena pyriformis, Tetrahymena pyriformis GL-7
brenda
Andersen, P.S.; Smith, J.M.; Mygind, B.
Characterization of the upp gene encoding uracil phosphoribosyltransferase of Escherichia coli K12
Eur. J. Biochem.
204
51-56
1992
Escherichia coli
brenda
Rasmussen, U.B.; Mygind, B.; Nygaard, P.
Purification and some properties of uracil phosphoribosyltransferase from Escherichia coli K12
Biochim. Biophys. Acta
881
268-275
1986
Escherichia coli, Escherichia coli SO 1344
brenda
McIvor, R.S.; Wohlhueter, R.M.; Plagemann, P.G.W.
Uracil phosphoribosyltransferase from Acholeplasma laidlawii: partial purification and kinetic properties
J. Bacteriol.
156
192-197
1983
Acholeplasma laidlawii
brenda
Lindsay, R.H.; Tillery, C.R.; Yu, M.Y.W.
Conversion of the antithyroid drug 2-thiouracil to 2-thio-5-UMP by UMP pyrophosphorylase
Arch. Biochem. Biophys.
148
466-474
1972
Lactobacillus leichmannii
brenda
Natalini, P.; Ruggieri, S.; Santarelli, I.; Vita, A.; Magni, G.
Bakers yeast UMP:pyrophosphate phosphoribosyltransferase. Purification, enzymatic and kinetic properties
J. Biol. Chem.
254
1558-1563
1979
Saccharomyces cerevisiae
brenda
Alloush, H.M.; Kerridge, D.
Characterization of a partially purified uracil phosphoribosyltransferase from the opportunistic pathogen Candida albicans
Mycopathologia
125
129-141
1994
Candida albicans
brenda
Carter, D.; Donald, R.G.K.; Roos, D.; Ullman, B.
Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii
Mol. Biochem. Parasitol.
87
137-144
1997
Toxoplasma gondii
brenda
Dai, Y.P.; Lee, C.S.; O'Sullivan, W.J.
Properties of uracil phosphoribosyltransferase from Giardia intestinalis
Int. J. Parasitol.
25
207-214
1995
Giardia duodenalis, Giardia duodenalis Portland
brenda
Jensen, K.F.; Mygind, B.
Different oligomeric states are involved in the allosteric behavior of uracil phosphoribosyltransferase from Escherichia coli
Eur. J. Biochem.
240
637-645
1996
Escherichia coli
brenda
Jensen, H.K.; Mikkelsen, N.; Neuhard, J.
Recombinant uracil phosphoribosyltransferase from the thermophile Bacillus caldolyticus: expression, purification, and partial characterization
Protein Expr. Purif.
10
356-364
1997
Bacillus subtilis, Bacillus subtilis 168, [Bacillus] caldolyticus (P70881), [Bacillus] caldolyticus
brenda
Grabner, G.K.; Switzer, R.L.
Kinetic studies of the uracil phosphoribosyltransferase reaction catalyzed by the Bacillus subtilis pyrimidine attenuation regulatory protein PyrR
J. Biol. Chem.
278
6921-6927
2003
Bacillus subtilis
brenda
Lundegaard, C.; Jensen, K.F.
Kinetic mechanism of uracil phosphoribosyltransferase from Escherichia coli and catalytic importance of the conserved proline in the PRPP binding site
Biochemistry
38
3327-3334
1999
Escherichia coli
brenda
Barchue, J.; Symersky, J.; Narayana, S.V.; Moore, J.K.; DeLucas, L.J.; Chattopadhyay, D.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of uracil phosphoribosyltransferase of Toxoplasma gondii
Acta Crystallogr. Sect. D
55
347-349
1999
Toxoplasma gondii (Q26998)
-
brenda
Schumacher, M.A.; Bashor, C.J.; Song, M.H.; Otsu, K.; Zhu, S.; Parry, R.J.; Ullman, B.; Brennan, R.G.
The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase
Proc. Natl. Acad. Sci. USA
99
78-83
2002
Toxoplasma gondii (Q26998), Toxoplasma gondii
brenda
Kadziola, A.; Neuhard, J.; Larsen, S.
Structure of product-bound Bacillus caldolyticus uracil phosphoribosyltransferase confirms ordered sequential substrate binding
Acta Crystallogr. Sect. D
58
936-945
2002
[Bacillus] caldolyticus (P70881), [Bacillus] caldolyticus
brenda
Arent, S.; Harris, P.; Jensen, K.F.; Larsen, S.
Allosteric regulation and communication between subunits in uracil phosphoribosyltransferase from Sulfolobus solfataricus
Biochemistry
44
883-892
2005
Saccharolobus solfataricus (Q980Q4), Saccharolobus solfataricus
brenda
Jensen, K.F.; Arent, S.; Larsen, S.; Schack, L.
Allosteric properties of the GTP activated and CTP inhibited uracil phosphoribosyltransferase from the thermoacidophilic archaeon Sulfolobus solfataricus
FEBS J.
272
1440-1453
2005
Saccharolobus solfataricus
brenda
Cleary, M.D.; Meiering, C.D.; Jan, E.; Guymon, R.; Boothroyd, J.C.
Biosynthetic labeling of RNA with uracil phosphoribosyltransferase allows cell-specific microarray analysis of mRNA synthesis and decay
Nat. Biotechnol.
23
232-237
2005
Toxoplasma gondii
brenda
O'Brien, T.A.; Tuong, D.T.; Basso, L.M.; McIvor, R.S.; Orchard, P.J.
Coexpression of the uracil phosphoribosyltransferase gene with a chimeric human nerve growth factor receptor/cytosine deaminase fusion gene, using a single retroviral vector, augments cytotoxicity of transduced human T cells exposed to 5-fluorocytosine
Hum. Gene Ther.
17
518-530
2006
Saccharomyces cerevisiae
brenda
Arsene-Ploetze, F.; Nicoloff, H.; Kammerer, B.; Martinussen, J.; Bringel, F.
Uracil salvage pathway in Lactobacillus plantarum: transcription and genetic studies
J. Bacteriol.
188
4777-4786
2006
Lactiplantibacillus plantarum (Q9RE01), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum BM604 (Q9RE01)
brenda
Khatri, A.; Zhang, B.; Doherty, E.; Chapman, J.; Ow, K.; Pwint, H.; Martiniello-Wilks, R.; Russell, P.J.
Combination of cytosine deaminase with uracil phosphoribosyl transferase leads to local and distant bystander effects against RM1 prostate cancer in mice
J. Gene Med.
8
1086-1096
2006
Mus musculus
brenda
Li, J.; Huang, S.; Chen, J.; Yang, Z.; Fei, X.; Zheng, M.; Ji, C.; Xie, Y.; Mao, Y.
Identification and characterization of human uracil phosphoribosyltransferase (UPRTase)
J. Hum. Genet.
52
415-422
2007
Homo sapiens, Homo sapiens (Q96BW1)
brenda
Islam, M.R.; Kim, H.; Kang, S.W.; Kim, J.S.; Jeong, Y.M.; Hwang, H.J.; Lee, S.Y.; Woo, J.C.; Kim, S.G.
Functional characterization of a gene encoding a dual domain for uridine kinase and uracil phosphoribosyltransferase in Arabidopsis thaliana
Plant Mol. Biol.
63
465-477
2007
Arabidopsis thaliana (Q9FKS0), Arabidopsis thaliana
brenda
Linde, L.; Jensen, K.F.
Uracil phosphoribosyltransferase from the extreme thermoacidophilic archaebacterium Sulfolobus shibatae is an allosteric enzyme, activated by GTP and inhibited by CTP.
Biochim. Biophys. Acta
1296
16-22
1996
Saccharolobus shibatae
brenda
Xing, L.; Deng, X.; Kotedia, K.; Ackerstaff, E.; Ponomarev, V.; Clifton Ling, C.; Koutcher, J.A.; Li, G.C.
Non-invasive molecular and functional imaging of cytosine deaminase and uracil phosphoribosyltransferase fused with red fluorescence protein
Acta Oncol.
47
1211-1220
2008
Homo sapiens (Q96BW1)
brenda
Perez-Zuniga, F.J.; Guenther Sillero, M.A.; Sillero, A.
Bisphosphonates activate the 5-fluorouracil/uracil phosphoribosyltransferase activity present in Saccharomyces cerevisiae cell extracts: implications for tumor treatments
Biochem. Pharmacol.
76
825-830
2008
Saccharomyces cerevisiae
brenda
Lu, S.; Wang, X.; Xiao, L.; Cai, L.; Zhang, Y.; Wang, H.; Wang, Z.
Gene therapy for ovarian cancer using adenovirus-mediated transfer of cytosine deaminase gene and uracil phosphoribosyltransferase gene directed by MDR1 promoter
Cancer Biol. Ther.
6
397-404
2007
Homo sapiens (Q96BW1)
brenda
Zeiner, G.M.; Cleary, M.D.; Fouts, A.E.; Meiring, C.D.; Mocarski, E.S.; Boothroyd, J.C.
RNA analysis by biosynthetic tagging using 4-thiouracil and uracil phosphoribosyltransferase
Methods Mol. Biol.
419
135-146
2008
Toxoplasma gondii (Q26998), Toxoplasma gondii
brenda
Gopinath, P.; Ghosh, S.S.
Apoptotic induction with bifunctional E.coli cytosine deaminase-uracil phosphoribosyltransferase mediated suicide gene therapy is synergized by curcumin treatment in vitro
Mol. Biotechnol.
39
39-48
2008
Escherichia coli
brenda
Fogar, P.; Navaglia, F.; Basso, D.; Greco, E.; Zambon, C.F.; Fadi, E.; Falda, A.; Stranges, A.; Vannozzi, F.; Danesi, R.; Pedrazzoli, S.; Plebani, M.
Suicide gene therapy with the yeast fusion gene cytosine deaminase/uracil phosphoribosyltransferase is not enough for pancreatic cancer
Pancreas
35
224-231
2007
Saccharomyces cerevisiae
brenda
Zhao, F.J.; Zhang, S.; Yu, Z.M.; Xia, S.J.; Li, H.
Specific targeting of prostate cancer cells in vitro by the suicide gene/prodrug system, uracil phosphoribosyltransferase/5-fluorouracil, under the control of prostate-specific membrane antigen promoter/enhancer
Prostate Cancer Prostatic. Dis.
12
166-171
2008
Escherichia coli
brenda
Tanaka, T.; Duflot-Dancer, A.; Tiraby, M.; Piccoli, C.; Tiraby, G.; Yamasaki, H.; Mesnil, M.
Bystander effect from cytosine deaminase and uracil phosphoribosyl transferase genes in vitro: a partial contribution of gap junctions
Cancer Lett.
282
43-47
2009
Homo sapiens
brenda
Christoffersen, S.; Kadziola, A.; Johansson, E.; Rasmussen, M.; Willemoes, M.; Jensen, K.F.
Structural and kinetic studies of the allosteric transition in Sulfolobus solfataricus uracil phosphoribosyltransferase: Permanent activation by engineering of the C-terminus
J. Mol. Biol.
393
464-477
2009
Saccharolobus solfataricus (Q980Q4), Saccharolobus solfataricus
brenda
Mainguet, S.E.; Gakiere, B.; Majira, A.; Pelletier, S.; Bringel, F.; Guerard, F.; Caboche, M.; Berthome, R.; Renou, J.P.
Uracil salvage is necessary for early Arabidopsis development
Plant J.
60
280-291
2009
Arabidopsis thaliana (Q9M336)
brenda
Altanerova, V.; Cihova, M.; Babic, M.; Rychly, B.; Ondicova, K.; Mravec, B.; Altaner, C.
Human adipose tissue-derived mesenchymal stem cells expressing yeast cytosinedeaminase:uracil phosphoribosyltransferase inhibit intracerebral rat glioblastoma
Int. J. Cancer
130
2455-2463
2012
Saccharomyces cerevisiae
brenda
Yata, V.; Sen, K.; Kumar, M.; Ghosh, S.
Interaction studies of E. coli uracil phosphoribosyltransferase with 5-fluorouracil for potent anti cancer activity
Med. Chem. Res.
21
1149-1155
2012
Escherichia coli
-
brenda
Ghode, P.; Jobichen, C.; Ramachandran, S.; Bifani, P.; Sivaraman, J.
Structural basis of mapping the spontaneous mutations with 5-flurouracil in uracil phosphoribosyltransferase from Mycobacterium tuberculosis
Biochem. Biophys. Res. Commun.
467
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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 ATCC 25618 (P9WFF3), Mycobacterium tuberculosis H37Rv (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 ATCC 10895 (Q754M0), Eremothecium gossypii CBS 109.51 (Q754M0), Eremothecium gossypii FGSC 9923 (Q754M0), Eremothecium gossypii NRRL Y-1056 (Q754M0)
brenda
Acosta, J.; Nguyen, K.; Spitale, R.C.; Fernandez-Lucas, J.
Taylor-made production of pyrimidine nucleoside-5'-monophosphate analogues by highly stabilized mutant uracil phosphoribosyltransferase from Toxoplasma gondii
Bioresour. Technol.
339
125649
2021
Toxoplasma gondii (Q26998)
brenda
Scherer, V.; Bellin, L.; Schwenkert, S.; Lehmann, M.; Rinne, J.; Witte, C.P.; Jahnke, K.; Richter, A.; Pruss, T.; Lau, A.; Waller, L.; Stein, S.; Leister, D.; Moehlmann, T.
Uracil phosphoribosyltransferase is required to establish a functional cytochrome b6f complex
Plant J.
120
1064-1078
2024
Arabidopsis thaliana
brenda
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