2.4.2.2: pyrimidine-nucleoside phosphorylase
This is an abbreviated version!
For detailed information about pyrimidine-nucleoside phosphorylase, go to the full flat file.
Word Map on EC 2.4.2.2
Reaction
Synonyms
AmPyNP, BbPyNP, BfPyNP, BsPyNP, deoA, EC 2.4.2.23, GsPyNP, GtPyNP, LpPyNP, nucleoside phosphorylase, PDP, phosphorylase, pyrimidine nucleoside, Py-NPase, PYNP, pynpase, pyrimidine nucleoside phosphorylase, pyrimidine ribonucleoside phosphorylase, pyrimidine-nucleoside phosphorylase, pyrimidine/purine nucleoside phosphorylase, TTHA1771, TtPyNP, udp, UPase
ECTree
2.4.2.2 pyrimidine-nucleoside phosphorylaseAdvanced search results
results (
results (General Information
General Information on EC 2.4.2.2 - pyrimidine-nucleoside phosphorylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
metabolism
uridine phosphorylase is a critical enzyme in pyrimidine salvage metabolism
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
additional information
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
evolution
the enzyme belongs to the NP family II
additional information
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
additional information
-
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
additional information
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
