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NP encodes an enzyme which reversibly catalyzes the phosphorolysis of purine nucleosides. Additionally we are shipping Nucleoside Phosphorylase Antibodies (47) and Nucleoside Phosphorylase Kits (12) and many more products for this protein.
Showing 9 out of 11 products:
Human NP Protein expressed in Escherichia coli (E. coli) - ABIN2005043
Canduri, Silva, dos Santos, Palma, Basso, Santos, de Azevedo: Structure of human PNP complexed with ligands. in Acta crystallographica. Section D, Biological crystallography 2005
Show all 2 references for ABIN2005043
Human NP Protein expressed in Escherichia coli (E. coli) - ABIN667267
Balakrishnan, Verma, OBrien, Kilpatrick, Chen, Tyler, Bickel, Bantia, Keating, Kantarjian, Gandhi, Ravandi: Phase 2 and pharmacodynamic study of oral forodesine in patients with advanced, fludarabine-treated chronic lymphocytic leukemia. in Blood 2010
Show all 2 references for ABIN667267
the biological role of packing of the PNP monomers into a trimeric structure
crystal structure complexed with analogs of the inhibitor 2-diaminopurine aglycone (purine nucleoside phosphorylase)
PNP purine nucleoside phosphorylase was crystallized in space group P2(1)2(1)2(1) in the presence of (S)-PMPDAP and phosphate, and the resulting structure of the binary PNP/(S)-PMPDAP complex was refined at 2.05A resolution.
alf (show GTF2A1L Proteins) spleen enzyme is a homotrimer and previous suggestions for dissociation of this enzyme into more active monomers, upon dilution of the enzyme or addition of phosphate, are incorrect.
PCR amplification of the calf phosphorylase from the calf spleen library, cloning, overexpression of the recombinant PNP, its enzymatic activity and interactions with typical ligands of mammalian wild type PNP are described.
The transition-state structure of triple mutant PNP is altered as a consequence of the amino acids in the second sphere from the catalytic site.
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.
the binding mechanism of a transition state analogue (DADMe-immucillin-H) to the purine nucleoside phosphorylase (PNP) enzyme, is reported.
Data show that [15N, 2H]His8-purine nucleoside phosphorylase (PNP) had reduced catalytic site chemistry larger than proportional to the enzymatic mass difference.
Study of genetic heterogeneity in systemic lupus erythematosus, the top associations in European ancestry were protein kinase (show CDK7 Proteins), cyclic GMP (show NT5C2 Proteins)-dependent, type I (PRKG1 (show PRKG1 Proteins)) rs7897633 (P(Meta) = 2.75 x 10(-8)) and purine nucleoside phosphorylase (PNP) rs1049564 (P(Meta) = 1.24 x 10(-7)).
Human small intestine is a key site for ribavirin phosphorolysis and that PNP is primarily involved in the metabolism.
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.
Biochemical and genetic data on a cohort of seven patients from six families identified as PNPase (show PNPT1 Proteins) deficient, is reported.
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.
investigation of catalytic mechanisms involved in catalysis by PNP: transition states in arsenolysis and phosphorolysis
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.
PNP deficiency causes cerebellar abnormalities, including Purkinje cell damage and progressive motor deficits.
PNP is important for the survival of DP thymocytes. Accumulation of dGuo in cases of PNP deficiency leads to mitochondria-initiated apoptosis of DP thymocytes, which can be prevented by restoring PNP activity in the cells.
This gene encodes an enzyme which reversibly catalyzes the phosphorolysis of purine nucleosides. The enzyme is trimeric, containing three identical subunits. Mutations which result in nucleoside phosphorylase deficiency result in defective T-cell (cell-mediated) immunity but can also affect B-cell immunity and antibody responses. Neurologic disorders may also be apparent in patients with immune defects. A known polymorphism at aa position 51 that does not affect enzyme activity has been described. A pseudogene has been identified on chromosome 2.
, inosine-guanosine phosphorylase
, nucleoside phosphorylase
, purine-nucleoside:orthophosphate ribosyltransferase
, purine nucleoside phosphorylase
, purine-nucleoside phosphorylase 1