purine nucleoside phosphorylase | Nucleoside synthesis and metabolism | IUPHAR/BPS Guide to PHARMACOLOGY

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purine nucleoside phosphorylase

Target not currently curated in GtoImmuPdb

Target id: 2841

Nomenclature: purine nucleoside phosphorylase

Abbreviated Name: PNP

Family: Nucleoside synthesis and metabolism, Purine-nucleoside phosphorylase

Annotation status:  image of a grey circle Awaiting annotation/under development. Please contact us if you can help with annotation.  » Email us

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 289 14q11.2 PNP purine nucleoside phosphorylase
Mouse - 289 14 B-C1 Pnp purine-nucleoside phosphorylase
Rat - 216 15p14 Pnp purine nucleoside phosphorylase
Gene and Protein Information Comments
The Antimalarial targets family provides information about P. falciparum PNP.
Previous and Unofficial Names
nucleoside phosphorylase | PUNP | NP
Database Links
ChEMBL Target
DrugBank Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
RefSeq Nucleotide
RefSeq Protein
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  Crystal structure of human PNP complexed with immucillin H.
PDB Id:  1PF7
Ligand:  forodesine
Resolution:  2.6Å
Species:  Human
References:  1
Enzyme Reaction
EC Number:
Description Reaction Reference
Purine-nucleoside phosphorylase Purine nucleoside + phosphate <=> purine + alpha-D-ribose 1-phosphate
Purine deoxynucleoside + phosphate <=> purine + 2'-deoxy-alpha-D-ribose 1-phosphate

Download all structure-activity data for this target as a CSV file

Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
forodesine Hs Inhibition 10.1 pKi 2
pKi 10.1 (Ki 7.2x10-11 M) [2]
Clinically-Relevant Mutations and Pathophysiology
Disease:  Purine nucleoside phosphorylase deficiency
Disease Ontology: DOID:5813
OMIM: 613179
Orphanet: ORPHA760
General Comments
PNP is required for the recycling of nucleosides and deoxynucleosides. In humans, PNP is the only route for degradation of deoxyguanosine. T cells are sensitive to deficiencies of this enzyme, and genetic deficiency of PNP causes loss of T cell function from birth and leads to significant immunodeficiency [3].


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1. Filgueira de Azevedo Jr W, Canduri F, Marangoni dos Santos D, Pereira JH, Dias MV, Silva RG, Mendes MA, Basso LA, Palma MS, Santos DS. (2003) Structural basis for inhibition of human PNP by immucillin-H. Biochem. Biophys. Res. Commun., 309 (4): 917-22. [PMID:13679061]

2. Miles RW, Tyler PC, Furneaux RH, Bagdassarian CK, Schramm VL. (1998) One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase. Biochemistry, 37 (24): 8615-21. [PMID:9628722]

3. Stoop JW, Zegers BJ, Hendrickx GF, van Heukelom LH, Staal GE, de Bree PK, Wadman SK, Ballieux RE. (1977) Purine nucleoside phosphorylase deficiency associated with selective cellular immunodeficiency. N. Engl. J. Med., 296 (12): 651-5. [PMID:402573]

How to cite this page

Nucleoside synthesis and metabolism: purine nucleoside phosphorylase. Last modified on 15/04/2019. Accessed on 22/02/2020. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2841.