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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.
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.
Data show that the mutations in purine nucleoside phosphorylase (PNP) alters the enthalpy-entropy balance with little effect on the catalytic rates.
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 (zeige CDK7 Proteine), cyclic GMP (zeige NT5C2 Proteine)-dependent, type I (PRKG1 (zeige PRKG1 Proteine)) 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 (zeige PNPT1 Proteine) deficient, is reported.
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 (zeige GTF2A1L Proteine) 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.
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
, purine-nucleoside:orthophosphate ribosyltransferase
, nucleoside phosphorylase
, purine nucleoside phosphorylase
, purine-nucleoside phosphorylase 1