EC Number   |
General Information |
Reference |
|---|
   2.4.2.2 | evolution |
pyrimidine-nucleoside phosphorylase is a member of the NP-II family, implying that it has a two-domain structure and functions as a dimer |
758599 |
| 2.4.2.2 | evolution |
the enzyme belongs to the NP family II |
758850 |
| 2.4.2.2 | malfunction |
inhibitors, such as 5-benzylacyclouridine (BAU), block the activity of uridine phosphorylase, inducing an increase in the plasma concentrations of uridine. This phenomenon, designated as uridine rescue, benefits the chemotherapeutic effect of 5-fluorouracil on colon cancer |
758699 |
| 2.4.2.2 | metabolism |
uridine phosphorylase is a critical enzyme in pyrimidine salvage metabolism |
758699 |
| 2.4.2.2 | more |
analysis of the three-dimensional structures of the nucleoside-binding sites in subunits A and B of BsPyNP complexed with imidazole. The imidazole (IMD) molecule is localized in the active site of both subunits. IMD interacts with the enzyme residues via hydrogen bonds and a stacking interaction |
758599 |
| 2.4.2.2 | more |
dynamic modelling of phosphorolytic cleavage catalyzed by pyrimidine-nucleoside phosphorylase, differential-dynamical model, kinetics, overview. Py-NPase-catalyzed phosphorylic cleavage reactions are reversible reactions proceeding towards a dynamic equilibrium. The reaction trajectory until equilibrium does not only depend on physical parameters, like temperature and pressure, but also on enzyme concentration, the concentration of substrates, or the presence of products |
760077 |
| 2.4.2.2 | physiological function |
the enzyme catalyzes reversible phosphorolysis of uridine to uracil and ribose-1-phosphate, and is responsible for maintenance of the uridine concentration in cells. Uridine phosphorylase is ubiquitously expressed in all living organisms, from bacteria to human, supporting an important role in cell survivability |
758699 |
