Recombinant Human Purine nucleoside phosphorylase (PNP)

1. The study suggests that mass-constrained femtosecond motions at the catalytic site of PNP can improve transition state barrier crossing by more frequent sampling of essential catalytic site contacts. PMID: 29915028
2. The PNP rs1049564 T allele is a loss-of-function variant that induces S-phase block and IFN pathway activation in lymphocytes. The S-phase block could be rescued in our in vitro experiments, suggesting the potential for personalized treatment. PMID: 28859258
3. Data show that the mutations in purine nucleoside phosphorylase (PNP) alters the enthalpy-entropy balance with little effect on the catalytic rates. PMID: 27976868
4. Data (including data from empirical valence bond/molecular dynamic simulations) suggest that PNP substrate specificity for inosine and guanosine is a direct result of electrostatic preorganization energy along the reaction coordinate. PMID: 26985580
5. the binding mechanism of a transition state analogue (DADMe-immucillin-H) to the purine nucleoside phosphorylase (PNP) enzyme, is reported. PMID: 25625196
6. Data show that [15N, 2H]His8-purine nucleoside phosphorylase (PNP) had reduced catalytic site chemistry larger than proportional to the enzymatic mass difference. PMID: 26305965
7. Study of genetic heterogeneity in systemic lupus erythematosus, the top associations in European ancestry were protein kinase, cyclic GMP-dependent, type I (PRKG1) rs7897633 (P(Meta) = 2.75 x 10(-8)) and purine nucleoside phosphorylase (PNP) rs1049564 (P(Meta) = 1.24 x 10(-7)). PMID: 25338677
8. Human small intestine is a key site for ribavirin phosphorolysis and that PNP is primarily involved in the metabolism. PMID: 24107682
9. insufficient data to evaluated impact of genetic polymorphisms on disease susceptibility PMID: 24792412
10. Complete lack of PNP triggers accumulation of deoxyguanosine, thereby disrupting B-cell development, the consequence of which is more profound with time, as was found in the older sister. PMID: 22578971
11. Biochemical and genetic data on a cohort of seven patients from six families identified as PNPase deficient, is reported. PMID: 22132981
12. This study for the first time describes elevated levels of alpha synuclein in pancreatic adenocarcinoma as well as highlights the potential of evaluating NP protein expression. PMID: 21448452
13. investigation of catalytic mechanisms involved in catalysis by PNP: transition states in arsenolysis and phosphorolysis PMID: 21348499
14. Results show that some regions, responsible for entrance and exit of substrate, present a conformational variability, which is dissected by dynamics simulation analysis. PMID: 19932753
15. PNP operating at maximum catalytic potential permits more rapid peptide amide deuterium exchange and greater conformational flexibility of water-peptide bond exchange rate than in either of the complexes with transition state analogues. PMID: 20108972
16. The optimum pH for PNP from human erythrocytes with xanthosine and xanthine is in the range 5-6, whereas those with guanosine, guanine, inosine & hypoxanthine are in the range 7-8. Possible PNP binding modes of Xan and Xao by mammalian PNPs are proposed. PMID: 12180982
17. Crystal structure of human purine nucleoside phosphorylase. PMID: 12914785
18. These data provide a framework in which to conduct genetic association studies of these two genes in relevant populations, thereby allowing hNP and hGSTO1-1 to be evaluated as potential susceptibility genes in human arsenicism. PMID: 12928150
19. investigation of the quaternary structure of recombinant human purine nucleoside phosphorylase PMID: 13679062
20. crystal structures in complex with inosine and 2',3'-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The structures provide explanation for ligand binding, refine the purine-binding site and can be used for future inhibitor design. PMID: 14706628
21. several recurring mutations were found in PNP in patients with purine nucleoside phosphorylase deficiency by DNA sequence analysis PMID: 15571269
22. crystal structure of human PNP in complex with hypoxanthine, refined to 2.6A resoluti PMID: 15582582
23. findings suggest that the G51S PNP polymorphism is associated with a faster rate of cognitive decline in Alzheimer's disease patients, highlighting the important role of purine metabolism in the progression of this neurodegenerative disorder PMID: 17221831
24. Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase PMID: 17639373
25. Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase. PMID: 18281956
26. New interactions caused by the mutations increase the catalytic efficiency of the enzyme for formation of a late transition state with increased participation of the phosphate nucleophile. PMID: 18281957
27. Structural studies on NP are reported with a view towards a new specific scoring function. PMID: 18790691
28. Protein dynamics on the femtosecond to picosecond timescale are linked to enzymatic function. PMID: 18946041
29. Comparative analysis of the model of BfPNP and the structure of HsPNP allowed identification of structural features responsible for differences in the computationally determined ligand affinities PMID: 19172318
30. Results describe a tryptophan-free mutant of purine nucleoside phosphorylase and its dynamic activity. PMID: 19191546
31. Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase PMID: 19425594

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HGNC: 7892

OMIM: 164050

KEGG: hsa:4860

STRING: 9606.ENSP00000354532

UniGene: Hs.75514