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Information on EC 2.4.2.3 - uridine phosphorylase and Organism(s) Homo sapiens and UniProt Accession Q16831

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.3 uridine phosphorylase
IUBMB Comments
The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. The mammalian enzyme also accepts 2'-deoxyuridine.
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This record set is specific for:
Homo sapiens
UNIPROT: Q16831
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
uridine phosphorylase, uph, upase, urdpase, uridine phosphorylase 1, pcup1, stuph, l-urdpase, vchuph, upase-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UP type 1
-
uridine phosphorylase 1
-
uridine phosphorylase-1
-
phosphorylase, uridine
-
-
-
-
pyrimidine phosphorylase
-
-
-
-
UDRPase
-
-
-
-
UPase
UPH
-
-
-
-
UrdPase
-
-
-
-
uridine phosphorylase-2
-
uridine:orthophosphate alpha-D-ribosyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
show the reaction diagram
ordered bi-bi mechanism, phosphate binds before uridine and alpha-D-ribose 1-phosphate is released after uracil
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
uridine:phosphate alpha-D-ribosyltransferase
The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. The mammalian enzyme also accepts 2'-deoxyuridine.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-22-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
uracil + alpha-D-ribose 1-phosphate
uridine + phosphate
show the reaction diagram
-
-
-
r
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
show the reaction diagram
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
show the reaction diagram
-
-
-
-
?
5'-deoxy-5-fluorouridine + alpha-D-ribose 1-phosphate
5'-deoxy-5-fluorouridine + phosphate
show the reaction diagram
-
-
-
-
?
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
?
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxy-D-ribose-1-phosphate
show the reaction diagram
-
-
also accepts 2'-deoxypyrimidine nucleosides in higher organisms
-
r
5-fluorouracil + alpha-D-ribose 1-phosphate
5-fluorouridine + phosphate
show the reaction diagram
-
-
-
-
?
5-fluorouracil + alpha-D-ribose-1-phosphate
5-fluorouridine + phosphate
show the reaction diagram
-
-
-
-
?
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose 1-phosphate
show the reaction diagram
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose-1-phosphate
show the reaction diagram
deoxyuridine + phosphate
uracil + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
?
thymidine + phosphate
thymine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
uracil + alpha-D-ribose 1-phosphate
uridine + phosphate
show the reaction diagram
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
uracil + alpha-D-ribose 1-phosphate
uridine + phosphate
show the reaction diagram
-
-
-
r
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
show the reaction diagram
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-benzyl-6-hydroxy-2-oxo-1,2-dihydropyridine-3-carbonitrile
2% inhibition at 0.001 mM
4-ethyl-6-hydroxy-2-oxo-1,2-dihydropyridine-3-carbonitrile
25% inhibition at 0.001 mM
4-hydroxy-5-[[(2-hydroxyethyl)amino]methyl]-3,4-dihydropyrimidin-2(1H)-one
2% inhibition at 0.001 mM
5-benzyl-1-(2'-hydroxyethoxymethyl)uracil
competitive inhibition with respect to uridine, noncompetitive inhibition with respect to phosphate
5-benzyl-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
43% inhibition at 0.001 mM
5-benzylacyclouridine
5-[(diethylamino)methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
25% inhibition at 0.001 mM
5-[(dimethylamino)methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
81% inhibition at 0.001 mM
5-[[(1,3-dihydroxypropan-2-yl)amino]methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
82% inhibition at 0.001 mM
5-[[(2,3-dihydroxypropyl)amino]methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
78% inhibition at 0.001 mM
6-hydroxy-1H-pyridin-2-one
38% inhibition at 0.001 mM
6-hydroxy-2-oxo-1,2-dihydropyridine-3-carbonitrile
67% inhibition at 0.001 mM
6-hydroxy-2-oxo-4-(propan-2-yl)-1,2-dihydropyridine-3-carbonitrile
31% inhibition at 0.001 mM
6-hydroxy-2-oxo-4-phenyl-1,2-dihydropyridine-3-carbonitrile
42% inhibition at 0.001 mM
6-hydroxy-2-oxo-4-propyl-1,2-dihydropyridine-3-carbonitrile
16% inhibition at 0.001 mM
6-hydroxy-3,4-dimethylpyridin-2(1H)-one
9.5% inhibition at 0.001 mM
6-hydroxy-3-methylpyridin-2(1H)-one
12% inhibition at 0.001 mM
6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
70% inhibition at 0.001 mM
6-hydroxy-4-methyl-2-oxo-5-phenyl-1,2-dihydropyridine-3-carbonitrile
12% inhibition at 0.001 mM
6-hydroxy-4-methyl-2-oxo-5-[(piperidin-1-yl)methyl]-1,2-dihydropyridine-3-carbonitrile
49% inhibition at 0.001 mM
6-hydroxy-4-methyl-5-[(morpholin-4-yl)methyl]-2-oxo-1,2-dihydropyridine-3-carbonitrile
51% inhibition at 0.001 mM
6-hydroxy-4-methylpyridin-2(1H)-one
16% inhibition at 0.001 mM
6-hydroxy-4-propyl-1H-pyridin-2-one-3-carbonitrile
16% inhibition at 0.001 mM
6-hydroxy-5-(((2-hydroxyethyl)amino)methyl)-4-methyl-1H-pyridin-2-one-3-carbonitrile
80% inhibition at 0.001 mM
alpha-D-ribose 1-phosphate
product inhibition pattern, noncompetitive versus uridine, competitive versus phosphate, overview
potassium 5-cyano-4-methyl-6-oxo-1,6-dihydropyridin-2-olate
60% inhibition at 0.001 mM
Uracil
product inhibition pattern, noncompetitive versus uridine and phosphate, overview
2'-deoxyglycosylthymine
-
-
2,2'-Anhydro-5-ethyluridine
-
-
2-deoxyglycosylthymine
-
-
5-(3'-Benzyloxybenzyl)-1-[(1'-aminomethyl-2'-hydroxyethoxy)methyl]uracil
-
-
5-benzylacyclouridine
5-bromoacyclouridine
-
-
5-fluoro-2'-deoxyuridine
-
-
5-fluoroacyclouridine
-
-
5-iodoacyclouridine
-
-
5-Substituted 2,2'-anhydrouridine
-
-
Acyclothymidine
-
competitive
acyclouridine
-
competitive
Benzylacyclouridines
-
Pyrimidine acyclonucleosides
-
competitive
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
phosphate
in 100 mMn Tris buffer pH 7.4, at 37°C
0.05
uridine
in 100 mMn Tris buffer pH 7.4, at 37°C
0.427
5-fluoro-2'-deoxyuridine
pH 7.4, 37°C
0.024
5-fluorouridine
pH 7.4, 37°C
0.3
deoxyuridine
pH 7.4, 37°C
0.13 - 0.279
phosphate
0.076
ribose 1-phosphate
-
-
0.073
thymidine
pH 7.4, 37°C
0.209
Uracil
-
-
0.076 - 0.242
uridine
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034 - 0.494
alpha-D-ribose 1-phosphate
0.05 - 0.137
Uracil
0.000025
2,2'-Anhydro-5-ethyluridine
-
-
0.005
2-deoxyglycosylthymine
-
-
0.000098 - 0.0073
5-benzylacyclouridine
0.013
5-bromoacyclouridine
-
-
0.014
5-fluoroacyclouridine
-
-
0.03
5-iodoacyclouridine
-
-
0.003
Acyclothymidine
-
-
0.015
acyclouridine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
recombinant enzyme,m pH profile, overview
7 - 7.75
-
pH 6.5: about 70% of activity maximum, pH 8.5: about 25% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UPP1 is significantly upregulated in glioma, especially in glioblastoma
Manually annotated by BRENDA team
UPP1 is significantly upregulated in glioma, especially in glioblastoma
Manually annotated by BRENDA team
UPP1 expression is significantly downregulated in thyroid cancer
Manually annotated by BRENDA team
Upase-2 is predominantly expressed in
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
peripheral, very low activity
Manually annotated by BRENDA team
additional information
-
present in all human tissue and tumors
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
significant upregulation of UPP1 in thyroid cancer tissues compared with normal thyroid tissues is significantly correlated with lymph node metastasis, tumour stage and tumour size. In the cell, reduced UPP1 expression significantly suppresses the migration, invasion and proliferation. Downregulation of UPP1 gene expression in TPC and BCPAP cells inhibits invasion and induces apoptosis in the thyroid cancer cells. Impact of UPP1 silencing on 5-fluorouracil (5-FU) chemo sensitivity in thyroid cancer cell lines
metabolism
physiological function
physiological function
-
the enzyme contributes to the antineoplastic activity of 5'-deoxy-5-fluorouridine. The peroxisome proliferator-activated receptor gamma coactivator-1alpha enhances antiproliferative activity of 5-deoxy-5-fluorouridine in cancer cells through induction of uridine phosphorylase, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UPP1_HUMAN
310
0
33934
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
4 * 33000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
isozyme UPP1, the N-terminus of the protein forms a strand-turn-strand structure bracketed by two short helices, structure, overview
homodimer
-
tetramer
-
4 * 33000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and enzyme in complex with inhibitor 5-benzylacyclouridine, 3 mg/ml protein in absence or presence of 1 mM inhibitor from 17% PEG 3350, 100 mM Bis-Tris buffer, pH 5.5, 300 mM KCl, and 30 mM MgCl2, or for the ligand-free enzyme crystals from 1.2 M (NH4)2SO4, 100 mM Bis-Tris buffer pH 5.5, with 1-2% MPD, with 2-3 mg/ml protein, X-ray diffraction structure determination and analysis at 2.3 A and 1.9 A resolution, respectively
in complex with 5-fluorouridine, to 2.3 A resolution. The dimeric enzyme is capable of a large hinge motion between its two domains, facilitating ligand exchange and explaining observed cooperativity between the two active sites in binding phosphate-bearing substrates. A loop toward the back end of the uracil binding pocket flexibly adjusts to the varying chemistry of different compounds through an ‘induced-fit association mechanism
two crystallographic structures of human isoform UPP2 in distinctly active and inactive conformations, to 2.0 and 1.54 A resolution, respectively. The structures reveal that a conditional intramolecular disulfide bridge can form within the protein that dislocates critical phosphate-coordinating arginine residue R100 away from the active site, disabling the enzyme. The state of the disulfide bridge has further structural consequences for one face of the enzyme that suggest UPP2 may have additional functions in sensing and initiating cellular responses to oxidative stress
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
enzyme UPP1 knockdown by siRNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged UPP1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant UP1 3.8fold from Escherichia coli strain Rosetta (DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
expression of the N-terminally His6-tagged UPP1 in Escherichia coli strain BL21(DE3)
expression of UP1 in Escherichia coli strain Rosetta (DE3)
gene UPP1, quantitative real-time quantitative PCR enzyme expression analysis
expressed in Colo-320TP1 and C26A cells
-
expression in Escherichia coli as a fusion protein to glutathione-S-transferase
fusion protein with maltose-binding protein
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
UPP1 expression is significantly downregulated in thyroid cancer
UPP1 is significantly upregulated in glioma, especially in glioblastoma
the peroxisome proliferator-activated receptor gamma coactivator-1alpha induces the enzyme in cancer cells via binding of a nuclear receptor, leading to enhanced antiproliferative activity of 5-deoxy-5-fluorouridine, overview. The activation is abolished by XCT790, i.e. 3-[4-(2,4-bis-trifluoromethylbenzyloxy)-3-methoxyphenyl]-2-cyano-N-(5-trifluoromethyl-1,3,4-thiadiazol-2-yl)acrylamide. Molecular mechanisms, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
drug development
UP12 is a target for development of enzyme inhibitors for cancer chemotherapy, design of inhibitors is intended to boost endogenous uridine levels to rescue normal tissues from the toxicity of fluoropyrimidine nucleoside chemotherapeutic agents, such as capecitabine and 5-fluorouracil.
medicine
-
the paired expression level of the uridine phosphorylase gene in gastric cancer is a possible prognostic marker for patients with 5-fluorouracil treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
el Kouni, M.H.; el Kouni, M.M.; Naguib, F.N.
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: implications for chemotherapy with 5-fluoropyrimidines
Cancer Res.
53
3687-3693
1993
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Pizzorno, G.; Cao, D.; Leffert, J.J.; Russell, R.L.; Zhang, D.; Handschumacher, R.E.
Homeostatic control of uridine and the role of uridine phosphorylase: a biological and clinical update
Biochim. Biophys. Acta
1587
133-144
2002
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Liu, M.; Cao, D.; Russell, R.; Handschumacher, R.E.; Pizzorno, G.
Expression, characterization, and detection of human uridine phosphorylase and identification of variant uridine phosphorolytic activity in selected human tumors
Cancer Res.
58
5418-5424
1998
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Niedzwicki, J.G.; El Kouni, M.H.; Chu, S.H.; Cha, S.
Pyrimidine acyclonucleosides, inhibitors of uridine phosphorylase
Biochem. Pharmacol.
30
2097-2101
1981
Homo sapiens
Manually annotated by BRENDA team
Veres, Z.; Szabolcs, A.; Szinai, I.; Denes, G.; Kajtar-Peredy, M.; Otvos, L.
5-Substituted-2,2-anhydrouridines, potent inhibitors of uridine phosphorylase
Biochem. Pharmacol.
34
1737-1740
1985
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Naguib, F.N.M.; El Kouni, M.H.; Chu, S.H.; Cha, S.
New analogues of benzylacyclouridines, specific and potent inhibitors of uridine phosphorylase from human and mouse livers
Biochem. Pharmacol.
36
2195-2201
1987
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Johansson, M.
Identification of a novel human uridine phosphorylase
Biochem. Biophys. Res. Commun.
307
41-46
2003
Mus musculus, Homo sapiens (O95045), Homo sapiens
Manually annotated by BRENDA team
Yano, S.; Kazuno, H.; Suzuki, N.; Emura, T.; Wierzba, K.; Yamashita, J.; Tada, Y.; Yamada, Y.; Fukushima, M.; Asao, T.
Synthesis and evaluation of 6-methylene-bridged uracil derivatives. Part 1: discovery of novel orally active inhibitors of human thymidine phosphorylase
Bioorg. Med. Chem.
12
3431-3441
2004
Bos taurus, Equus caballus, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Yan, R.; Wan, L.; Pizzorno, G.; Cao, D.
Uridine phosphorylase in breast cancer: a new prognostic factor?
Front. Biosci.
11
2759-2766
2006
Gallus gallus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Temmink, O.H.; de Bruin, M.; Laan, A.C.; Turksma, A.W.; Cricca, S.; Masterson, A.J.; Noordhuis, P.; Peters, G.J.
The role of thymidine phosphorylase and uridine phosphorylase in (fluoro)pyrimidine metabolism in peripheral blood mononuclear cells
Int. J. Biochem. Cell Biol.
38
1759-1765
2006
Homo sapiens
Manually annotated by BRENDA team
Temmink, O.H.; de Bruin, M.; Turksma, A.W.; Cricca, S.; Laan, A.C.; Peters, G.J.
Activity and substrate specificity of pyrimidine phosphorylases and their role in fluoropyrimidine sensitivity in colon cancer cell lines
Int. J. Biochem. Cell Biol.
39
565-575
2007
Homo sapiens
Manually annotated by BRENDA team
Balestri, F.; Barsotti, C.; Lutzemberger, L.; Camici, M.; Ipata, P.L.
Key role of uridine kinase and uridine phosphorylase in the homeostatic regulation of purine and pyrimidine salvage in brain
Neurochem. Int.
51
517-523
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kawamura, K.; Takiguchi, N.; Wada, A.; Takenobu, H.; Kimura, H.; Soda, H.; Nagata, M.; Asano, T.; Tagawa, M.
Up-regulated expression of the uridine phosphorylase gene in human gastric tumors is correlated with a favorable prognosis
Anticancer Res.
26
4647-4651
2007
Homo sapiens
Manually annotated by BRENDA team
Renck, D.; Ducati, R.G.; Palma, M.S.; Santos, D.S.; Basso, L.A.
The kinetic mechanism of human uridine phosphorylase 1: Towards the development of enzyme inhibitors for cancer chemotherapy
Arch. Biochem. Biophys.
497
35-42
2010
Homo sapiens (Q16831), Homo sapiens
Manually annotated by BRENDA team
Roosild, T.P.; Castronovo, S.; Fabbiani, M.; Pizzorno, G.
Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy
BMC Struct. Biol.
9
14
2009
Homo sapiens (Q16831), Homo sapiens
Manually annotated by BRENDA team
Kong, X.; Fan, H.; Liu, X.; Wang, R.; Liang, J.; Gupta, N.; Chen, Y.; Fang, F.; Chang, Y.
Peroxisome proliferator-activated receptor gamma coactivator-1alpha enhances antiproliferative activity of 5-deoxy-5-fluorouridine in cancer cells through induction of uridine phosphorylase
Mol. Pharmacol.
76
854-860
2009
Homo sapiens
Manually annotated by BRENDA team
Roosild, T.P.; Castronovo, S.; Villoso, A.; Ziemba, A.; Pizzorno, G.
A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity
J. Struct. Biol.
176
229-237
2011
Homo sapiens (O95045), Homo sapiens
Manually annotated by BRENDA team
Roosild, T.; Castronovo, S.
Active site conformational dynamics in human uridine phosphorylase 1
PLoS ONE
5
e12741
2010
Homo sapiens (Q16831), Homo sapiens
Manually annotated by BRENDA team
Renck, D.; Machado, P.; Souto, A.A.; Rosado, L.A.; Erig, T.; Campos, M.M.; Farias, C.B.; Roesler, R.; Timmers, L.F.; de Souza, O.N.; Santos, D.S.; Basso, L.A.
Design of novel potent inhibitors of human uridine phosphorylase-1: synthesis, inhibition studies, thermodynamics, and in vitro influence on 5-fluorouracil cytotoxicity
J. Med. Chem.
56
8892-8902
2013
Homo sapiens (Q16831), Homo sapiens
Manually annotated by BRENDA team
Wang, J.; Xu, S.; Lv, W.; Shi, F.; Mei, S.; Shan, A.; Xu, J.; Yang, Y.
Uridine phosphorylase 1 is a novel immune-related target and predicts worse survival in brain glioma
Cancer Med.
9
5940-5947
2020
Homo sapiens (Q16831), Homo sapiens
Manually annotated by BRENDA team
Guan, Y.; Bhandari, A.; Zhang, X.; Wang, O.
Uridine phosphorylase 1 associates to biological and clinical significance in thyroid carcinoma cell lines
J. Cell. Mol. Med.
23
7438-7448
2019
Homo sapiens (Q16831)
Manually annotated by BRENDA team