2.4.2.3: uridine phosphorylase
This is an abbreviated version!
For detailed information about uridine phosphorylase, go to the full flat file.
Word Map on EC 2.4.2.3
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2.4.2.3
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pyrimidine
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nucleoside
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thymidine
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uracil
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5-fluorouracil
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phosphorolysis
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salvage
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orotate
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phosphoribosyltransferase
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phosphorylases
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thymidylate
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fluoropyrimidine
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udp
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5'-deoxy-5-fluorouridine
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5-fluoro-2'-deoxyuridine
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dihydropyrimidine
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acyclonucleoside
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5-fluorouridine
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ribose-1-phosphate
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capecitabine
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5-methyluridine
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dthdpase
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fdurd
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orotidine
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dihydrouracil
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uridine-cytidine
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mete
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diagnostics
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medicine
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synthesis
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drug development
- 2.4.2.3
- pyrimidine
- nucleoside
- thymidine
- uracil
- 5-fluorouracil
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phosphorolysis
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salvage
- orotate
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phosphoribosyltransferase
- phosphorylases
- thymidylate
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fluoropyrimidine
- udp
- 5'-deoxy-5-fluorouridine
- 5-fluoro-2'-deoxyuridine
- dihydropyrimidine
- acyclonucleoside
- 5-fluorouridine
- ribose-1-phosphate
- capecitabine
- 5-methyluridine
- dthdpase
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fdurd
- orotidine
- dihydrouracil
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uridine-cytidine
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mete
- diagnostics
- medicine
- synthesis
- drug development
Reaction
Synonyms
apUP, EC 2.4.2.23, L-UrdPase, More, PcUP1, PcUP2, phosphorylase, uridine, pynpase, pyrimidine nucleoside phosphorylase, pyrimidine phosphorylase, pyrimidine/purine nucleoside phosphorylase, StUPh, udp, UDRPase
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2.4.2.3 uridine phosphorylaseAdvanced search results
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General Information on EC 2.4.2.3 - uridine phosphorylase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
additional information
evolution
phylogenetic analysis of UPs in oomycetes
metabolism
uridine phosphorylase is a key enzyme in the pyrimidine salvage pathway, catalyzing the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate
metabolism
uridine phosphorylase is a ubiquitous enzyme involved in pyrimidine salvage and maintenance of uridine homeostasis
metabolism
uridine phosphorylase (UP) is a key enzyme of pyrimidine salvage pathways that enables the recycling of endogenous or exogenous-supplied pyrimidines and plays an important intracellular metabolic role
metabolism
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uridine phosphorylase (UP) is a key enzyme of pyrimidine salvage pathways that enables the recycling of endogenous or exogenous-supplied pyrimidines and plays an important intracellular metabolic role
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physiological function
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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
physiological function
uridine phosphorylase is a ubiquitous enzyme involved in pyrimidine salvage and maintenance of uridine homeostasis. UPP1 plays a role in the activation of pyrimidine nucleoside analogues used in chemotherapy, such as 5-fluorouracil and its prodrug, capecitabine
physiological function
enzyme UPP1 plays an essential role in pyrimidine salvage and regulation of uridine homeostasis. It plays a vital role in the stimulation of pyrimidine nucleoside analogues. UPP1 expression effects on 5-fluorouracil regulates epithelial-mesenchymal transition pathway. UPP1 acts as a crucial oncogene in thyroid cancer regulating epithelial-mesenchymal transition. Upregulation of UPP1 increases lymph node metastasis risk
physiological function
UPP1 interacts with immune checkpoint members in glioma
physiological function
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uridine phosphorylase (UPh) is the enzyme that catalyzes the synthesis of thymidine or 5-methyluridine from thymine, as well as their phosphorolysis
additional information
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bacterial thymidine phosphorylases of the NP-II family cannot bind 6-methyluracil in a proper conformation required for the catalysis because of a close contact between the 6-methyl group and Phe210. Structure-function analysis, overview
additional information
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enzyme structure modeling, molecular dynamics simulation, overview. Calculation of the protein-ligand binding free energy
additional information
strict conservation of UP1 key residues in the binding pocket, structure analysis of PcUP1 with bound ligands, active site structure and substrate binding, overview
additional information
strict conservation of UP1 key residues in the binding pocket, structure analysis of PcUP1 with bound ligands, active site structure and substrate binding, overview
additional information
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strict conservation of UP1 key residues in the binding pocket, structure analysis of PcUP1 with bound ligands, active site structure and substrate binding, overview
additional information
structure of the active center of enzyme UDP from Shewanella oneidensis strain MR-1 (SoUDP) in complex with uridine and sulfate (code PDB 4R2W), structure-function analysis. In the SoUDP active center, uridine is in high-energy syn-conformation, and the ribose residue acquires a conformation close to planar
additional information
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the formation of a hydrogen-bond network between the 2'-hydroxy group of uridine and atoms of the active-site residues of uridine phosphorylase leads to conformational changes of the ribose moiety of uridine, resulting in an increase in the reactivity of uridine compared to thymidine. Since the binding of thymidine to residues of uridine phosphorylase causes a smaller local strain of the beta-N1-glycosidic bond in this the substrate compared to the uridine molecule, the beta-N1-glycosidic bond in thymidine is more stable and less reactive than that in uridine. The phosphate anion, which is the second substrate bound at the active site, interacts simultaneously with the residues of the beta5-strand and the beta1-strand through hydrogen bonding, thus securing the gate loop in a conformation so that the active site of the enzyme molecule becomes inaccessible for nucleoside binding. Structures of VchUPh in complexes with thymine and uracil are prepared for molecular docking of the second substrates of the reverse reaction (ribose 1-phosphate and 2-deoxyribose 1-phosphate). The phosphate-binding F site of the EF homodimer of VchUPh is formed by hydrophilic residues, four of which belong to the F subunit (Thr93/F, Gly25/F, Arg29/F, and Arg90/F), and the fifth residue (Arg47/E) belongs to the E subunit. Residues Gln165, Arg167, and Arg222 play key roles in the binding of the pyrimidine moiety of the ligand (uridine, thymidine, uracil, and thymine) to VchUPh. Residues Glu197 and Thr93, as well as His7 of the adjacent subunit, play the main role in the binding of the furanose moiety of thymidine and uridine. The uridine (URI) molecule occupies the whole nucleoside-binding site of the VchUPh molecule. The URI molecule interacts with the nucleoside-binding site in the structure of VchUPh complexed with uridine (ID PDB: 5C80) through hydrogen bonds
additional information
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strict conservation of UP1 key residues in the binding pocket, structure analysis of PcUP1 with bound ligands, active site structure and substrate binding, overview
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