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Identification
HMDB Protein ID HMDBP03752
Secondary Accession Numbers
  • 9340
Name Purine nucleoside phosphorylase
Synonyms
  1. Inosine phosphorylase
  2. PNP
  3. Inosine-guanosine phosphorylase
Gene Name PNP
Protein Type Enzyme
Biological Properties
General Function Involved in purine-nucleoside phosphorylase activity
Specific Function The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Pathways
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Azathioprine Action Pathway
  • Gout or Kelley-Seegmiller Syndrome
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mitochondrial DNA depletion syndrome
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • Nicotinate and Nicotinamide Metabolism
  • Nicotinate and nicotinamide metabolism
  • Purine Metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • purine nucleoside salvage
  • Pyrimidine metabolism
  • Thioguanine Action Pathway
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Reactions
Nebularine + Phosphoric acid → Purine + Ribose 1-phosphate details
Adenosine + Phosphoric acid → Adenine + Ribose 1-phosphate details
Inosine + Phosphoric acid → Hypoxanthine + Ribose 1-phosphate details
Deoxyguanosine + Phosphoric acid → Guanine + Deoxyribose 1-phosphate details
Guanosine + Phosphoric acid → Guanine + Ribose 1-phosphate details
Nicotinamide riboside + Phosphoric acid → Niacinamide + Ribose 1-phosphate details
Nicotinate D-ribonucleoside + Phosphoric acid → Nicotinic acid + Ribose 1-phosphate + Hydrogen Ion details
Xanthosine + Phosphoric acid → Xanthine + Ribose 1-phosphate details
Deoxyuridine + Phosphoric acid → Uracil + Deoxyribose 1-phosphate details
Deoxyadenosine + Phosphoric acid → Adenine + Deoxyribose 1-phosphate details
Deoxyinosine + Phosphoric acid → Hypoxanthine + Deoxyribose 1-phosphate details
GO Classification
Biological Process
purine nucleobase metabolic process
purine nucleotide catabolic process
positive regulation of T cell proliferation
purine-containing compound salvage
response to drug
immune response
inosine catabolic process
NAD biosynthesis via nicotinamide riboside salvage pathway
nicotinamide riboside catabolic process
urate biosynthetic process
positive regulation of alpha-beta T cell differentiation
interleukin-2 secretion
Cellular Component
cytosol
cytoskeleton
Function
catalytic activity
transferase activity
transferase activity, transferring pentosyl groups
transferase activity, transferring glycosyl groups
purine-nucleoside phosphorylase activity
Molecular Function
nucleoside binding
purine nucleobase binding
purine-nucleoside phosphorylase activity
drug binding
phosphate ion binding
Process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside metabolic process
Cellular Location
  1. Cytoplasm
  2. cytoskeleton
Gene Properties
Chromosome Location 14
Locus 14q13.1
SNPs PNP
Gene Sequence
>870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Protein Properties
Number of Residues 289
Molecular Weight 32117.69
Theoretical pI 6.943
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
GenBank ID Protein 35565
UniProtKB/Swiss-Prot ID P00491
UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN
PDB IDs
GenBank Gene ID X00737
GeneCard ID PNP
GenAtlas ID PNP
HGNC ID HGNC:7892
References
General References
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  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed:12928150 ]
  6. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed:6087295 ]
  7. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed:3029074 ]
  8. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed:2104852 ]
  9. Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed:1384322 ]
  10. Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed:8931706 ]