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Symmetric Nucleosides as Potent Purine Nucleoside Phosphorylase Inhibitors
The Journal of Physical Chemistry B, 2021Nucleic acids are one of the most enigmatic biomolecules crucial to several biological processes. Nucleic acid-protein interactions are vital for the coordinated and controlled functioning of a cell, leading to the design of several nucleoside/nucleotide analogues capable of mimicking these interactions and hold paramount importance in the field of ...
Pradeep Pant, Amita Pathak, B. Jayaram
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Vanadate as a new substrate for nucleoside phosphorylases
Journal of Biological Inorganic Chemistry, 2022Orthovanadate was shown to serve as a substrate for nucleoside phosphorylases from Escherichia coli, Shewanella oneidensis, Geobacillus stearothermophilus, and Halomonas chromatireducens AGD 8-3. An exception is thymidine phosphorylase from the extremophilic haloalkaliphilic bacterium Halomonas chromatireducens AGD 8-3, which cannot catalyze the ...
Alexey N Antipov
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Oligomeric Symmetry of Purine Nucleoside Phosphorylases
SymmetryMany enzymes are composed of several identical subunits, which are arranged in a regular fashion and usually comply with some definite symmetry. This symmetry may be approximate or exact and may or may not coincide with the symmetry of crystallographic packing.
Boris Gomaz, Zoran Stefanic
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Biosynthesis of nucleoside analogues via thermostable nucleoside phosphorylase
Applied Microbiology and Biotechnology, 2012Biocatalyzed synthesis of nucleoside analogues was carried out using two thermostable nucleoside phosphorylases from the hyperthermophilic aerobic crenarchaeon Aeropyrum pernix K1. The synthesis of the 2,6-diaminopurine nucleoside and 5-methyluridine was used as a reaction model to test the process.
Shaozhou, Zhu +6 more
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Allosteric regulation of purine nucleoside phosphorylase
Archives of Biochemistry and Biophysics, 1991Purine nucleoside phosphorylase (EC 2.4.2.1) from bovine spleen is allosterically regulated. With the substrate inosine the enzyme displayed complex kinetics: positive cooperativity vs inosine when this substrate was close to physiological concentrations, negative cooperativity at inosine concentrations greater than 60 microM, and substrate inhibition ...
P A, Ropp, T W, Traut
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Inherited variants of human nucleoside phosphorylase
Annals of Human Genetics, 1971SUMMARY1. A method, for the starch gel electrophoresis of human nucleoside phosphorylase (NP) is described. Multiple NP isozymes were found in most human tissues and the best resolution of these isozymes was achieved by electrophoresis in a buffer system containing lithium ions.2.
Y H, Edwards, D A, Hopkinson, H, Harris
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Purine nucleoside phosphorylase of chicken liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Abstract Purine nucleoside phosphorylase (purine nucleoside:orthophosphate ribosyltransferase, EC 2.4.2.1) has been purified 125-fold from the homogenate of chicken livers and some of the properties of the purified enzyme have been studied. This enzyme had a pH optimum at around 6.o. At high substrate levels of inosine the reaction rate was increased,
K, Murakami, A, Mitsui, K, Tsushima
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Characterization of purine nucleoside phosphorylase in leukemia
American Journal of Hematology, 1986AbstractPurine nucleoside phosphorylase (PNP) activity was determined in mononuclear cells from 49 patients with various types of leukemia. A low level of PNP activity was found in mononuclear cells from patients with acute myeloid and lymphoblastic leukemia and with chronic lymphocytic leukemia. Enzymatic and immunological studies on PNP from leukemic
T, Morisaki +3 more
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Adenine as Substrate for Purine Nucleoside Phosphorylase
Canadian Journal of Biochemistry, 1971Purine nucleoside phosphorylase (purine-nucleoside:orthophosphate ribosyltransferase, EC 2.4.2.1) from four sources (rat liver and brain, human erythrocytes, and calf spleen) has been shown to exhibit a low intrinsic activity towards adenine in the presence of ribose 1-phosphate.
T P, Zimmerman +3 more
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