EC Number   |
General Information |
Reference |
|---|
    2.4.2.3 | evolution |
phylogenetic analysis of UPs in oomycetes |
-, 760136 |
| 2.4.2.3 | evolution |
the enzyme belongs to the NP-I family of uridine phosphorylases |
759090 |
| 2.4.2.3 | 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 |
759543 |
| 2.4.2.3 | 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 |
-, 760136 |
| 2.4.2.3 | metabolism |
uridine phosphorylase is a key enzyme in the pyrimidine salvage pathway, catalyzing the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate |
701939 |
| 2.4.2.3 | metabolism |
uridine phosphorylase is a ubiquitous enzyme involved in pyrimidine salvage and maintenance of uridine homeostasis |
702929 |
| 2.4.2.3 | more |
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 |
759090 |
| 2.4.2.3 | more |
enzyme structure modeling, molecular dynamics simulation, overview. Calculation of the protein-ligand binding free energy |
759091 |
| 2.4.2.3 | more |
strict conservation of UP1 key residues in the binding pocket, structure analysis of PcUP1 with bound ligands, active site structure and substrate binding, overview |
-, 760136 |
| 2.4.2.3 | more |
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 |
758663 |
