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Information on EC 2.4.2.1 - purine-nucleoside phosphorylase and Organism(s) Plasmodium falciparum and UniProt Accession Q8T9Z7
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2.4.2.1 purine-nucleoside phosphorylaseIUBMB Comments
Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase.
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Word Map
- 2.4.2.1
- p-nitrophenol
- deaminase
- polynucleotide
- lymphocyte
- hypoxanthine
-
phosphorolysis
- rnase
-
salvage
- guanine
-
paraneoplastic
- t-cells
- pemphigus
- immunodeficiency
-
pincer
- deoxyguanosine
- exoribonuclease
- phosphoribosyltransferase
- polyneuropathy
- 5'-nucleotidase
-
practitioner
- dgtp
- nurse
-
degradosome
-
hypoxanthine-guanine
- parathion
- blister
-
bullous
-
mucocutaneous
- ribonucleosides
-
desmogleins
- deoxynucleosides
- deoxycytidine
- hgprt
-
phrenic
- castleman
- deoxyadenosine
- 2'-deoxyguanosine
-
metal-ligand
- obliterans
- pneumoperitoneum
- desmoplakins
- pemphigoid
-
square-planar
-
photocatalysts
- lesch-nyhan
-
iridium
-
photocatalytic
- acantholysis
- medicine
-
exonucleolytic
- p-aminophenol
- drug development
- analysis
- pharmacology
- synthesis
The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pnp, purine nucleoside phosphorylase, pnpase, pfpnp, purine-nucleoside phosphorylase, adenosine phosphorylase, hspnp, hppnp, tvpnp, inosine phosphorylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine phosphorylase
-
-
-
-
inosine phosphorylase
-
-
-
-
inosine-guanosine phosphorylase
-
-
-
-
nucleotide phosphatase (2.4.2.1)
-
-
-
-
PfPNP
phosphorylase, purine nucleoside
-
-
-
-
PNP
PNPase
-
-
-
-
Pu-NPase
-
-
-
-
PUNP
-
-
-
-
PUNPI
-
-
-
-
PUNPII
-
-
-
-
purine deoxynucleoside phosphorylase
-
-
-
-
purine deoxyribonucleoside phosphorylase
-
-
-
-
purine nucleoside phosphorylase
purine ribonucleoside phosphorylase
-
-
-
-
purine nucleoside phosphorylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
purine-nucleoside:phosphate ribosyltransferase
Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase.
CAS REGISTRY NUMBER
COMMENTARY
9030-21-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-alpha-D-ribose 1-phosphate
-
-
-
?
deoxyinosine + phosphate
hypoxanthine + alpha-D-deoxyribose 1-phosphate
-
-
-
?
2'-deoxyinosine + phosphate
alpha-D-2-deoxyribose 1-phosphate + hypoxanthine
-
-
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
-
-
-
r
deoxyguanosine + phosphate
guanine + alpha-D-deoxyribose 1-phosphate
-
-
-
-
?
methylthioinosine + phosphate
methylthiohypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
-
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
-
-
-
r
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
ver low activity
-
-
?
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
r
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
-
-
-
-
?
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
-
-
-
r
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
-
r
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
-
-
-
r
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
-
-
-
r
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
weak binding inhibitor
1-((2-pyrrolidine-1-yl)ethyl)uracil
inhibits both enzymic activity and growth of Plasmodium falciparum
3-((2-pyrrolidine-1-yl)ethyl)uracil
inhibits both enzymic activity and growth of Plasmodium falciparum
5'-methylthio-immucillin-H
-
favours inhibition of Plasmodium falciparum purine nucleoside phosphorylase over human enzyme
5'-methylthio-immucillin-H
a potent and selective inhibitor of PfPNP. Imucillins are known inhibitors of PfPNP
additional information
-
the enzyme inhibitors 8-amino-5'-deoxy-5'-chloroguanosine and 8-amino-9-benzylguanine may have some antimalarial potential by limiting hypoxanthine production in the parasite-infected erythrocyte
-
additional information
pharmacophore-based virtual screening coupled to a consensual molecular docking approach is used to identify 59 potential PfPNP inhibitors that are predicted to be orally absorbed in a Caco-2 cell model. Superposition of the bioactive conformations of 5'-methylthioimmucillin-H (PDB ID 1Q1G) and DADMe-immucillin-G (PDB ID 3PHC). Inhibitor docking analysis, kinetics, and binding structures, overview. Molecular dynamics simulations
-
additional information
-
pharmacophore-based virtual screening coupled to a consensual molecular docking approach is used to identify 59 potential PfPNP inhibitors that are predicted to be orally absorbed in a Caco-2 cell model. Superposition of the bioactive conformations of 5'-methylthioimmucillin-H (PDB ID 1Q1G) and DADMe-immucillin-G (PDB ID 3PHC). Inhibitor docking analysis, kinetics, and binding structures, overview. Molecular dynamics simulations
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0088
5'-methylthioinosine
wild type enzyme, at pH 7.4, temperature not specified in the publication
0.011
5'-methylthioinosine
mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication
0.011
5'-methylthioinosine
mutant enzyme V73I, at pH 7.4, temperature not specified in the publication
0.012
5'-methylthioinosine
mutant enzyme V66I, at pH 7.4, temperature not specified in the publication
0.015
5'-methylthioinosine
mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication
0.018
5'-methylthioinosine
mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication
0.044
5'-methylthioinosine
mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication
0.06
5'-methylthioinosine
mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication
0.0025
Inosine
mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication
0.0036
Inosine
mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication
0.004
Inosine
mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication
0.0062
Inosine
mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication
0.011
Inosine
wild type enzyme, at pH 7.4, temperature not specified in the publication
0.013
Inosine
mutant enzyme V73I, at pH 7.4, temperature not specified in the publication
0.016
Inosine
mutant enzyme V66I, at pH 7.4, temperature not specified in the publication
0.028
Inosine
mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
5'-methylthioinosine
mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication
0.05
5'-methylthioinosine
mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication
0.28
5'-methylthioinosine
mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication
0.3
5'-methylthioinosine
mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication
0.81
5'-methylthioinosine
mutant enzyme V73I, at pH 7.4, temperature not specified in the publication
0.83
5'-methylthioinosine
wild type enzyme, at pH 7.4, temperature not specified in the publication
0.91
5'-methylthioinosine
mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication
1.2
5'-methylthioinosine
mutant enzyme V66I, at pH 7.4, temperature not specified in the publication
0.21
Inosine
mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication
0.36
Inosine
mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication
0.59
Inosine
mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication
1.2
Inosine
mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication
1.7
Inosine
wild type enzyme, at pH 7.4, temperature not specified in the publication
1.9
Inosine
mutant enzyme V73I, at pH 7.4, temperature not specified in the publication
2
Inosine
mutant enzyme V66I, at pH 7.4, temperature not specified in the publication
4.6
Inosine
mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.56
5'-methylthioinosine
mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication
4.6
5'-methylthioinosine
mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication
4.7
5'-methylthioinosine
mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication
6.8
5'-methylthioinosine
mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication
62
5'-methylthioinosine
mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication
71
5'-methylthioinosine
mutant enzyme V73I, at pH 7.4, temperature not specified in the publication
94
5'-methylthioinosine
mutant enzyme V66I, at pH 7.4, temperature not specified in the publication
95
5'-methylthioinosine
wild type enzyme, at pH 7.4, temperature not specified in the publication
83
Inosine
mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication
90
Inosine
mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication
130
Inosine
mutant enzyme V66I, at pH 7.4, temperature not specified in the publication
140
Inosine
mutant enzyme V73I, at pH 7.4, temperature not specified in the publication
150
Inosine
wild type enzyme, at pH 7.4, temperature not specified in the publication
160
Inosine
mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication
170
Inosine
mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication
190
Inosine
mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000018
5'-methylthio-immucillin H
pH 7.4, temperature not specified in the publication
0.0000027
5'-methylthio-immucillin-H
pH 7.4, equilibrium inhibition constant
0.000015
immucillin H
pH 7.4, temperature not specified in the publication
0.6
1',9-methyl-immucillin-H
-
Ki above 0.6 mM, pH 7.4, temperature not specified in the publication
0.0000019
2'-deoxy-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.0000009
4'-deaza-1'-aza-2'-deoxy-1',9-methyl-immucillin-G
-
pH 7.4, temperature not specified in the publication
0.0000005
4'-deaza-1'-aza-2'-deoxy-1',9-methyl-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.00022
5'-amido-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.000017
5'-carboxy-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.0000016
5'-deoxy-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.0000022
5'-fluoro-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.00000027
5'-methylthio-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.000000093
5'-thio-immucillin-H
-
pH 7.4, temperature not specified in the publication
0.00000086
immucillin-H
-
pH 7.4, temperature not specified in the publication
0.0000074
deoxyimmucillin-H
pH 7.4, equilibrium inhibition constant
0.00013
deoxyimmucillin-H
pH 7.4, inhibition constant during slow-onset phase
0.000029
immucillin-H
pH 7.4, inhibition constant during slow-onset phase
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0009
5'-methylthio-immucillin-H
Plasmodium falciparum
gene disruption mutant, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
targeted gene disruption results in loss of enzyme activity in lysate, with normal activity of adenosine deaminase. Mutant parasites show a greater requirement for exogenous purines and a severe growth defect at physiological concentrations of hypoxanthine. The mutant parasites are more sensitive to purine nucleoside phosphorylase inhibitors that bind human purine nucelotide phosphorylase tighter and less sensitive to inhibitor 5'-methylthio-immucillin-H
metabolism
the enzyme is involved in the purine metabolism in Plasmodium falciparum
additional information
additional information
superposition of the bioactive conformations of 5'-methylthioimmucillin-H (PDB ID 1Q1G) and DADMe-immucillin-G (PDB ID 3PHC)
additional information
-
superposition of the bioactive conformations of 5'-methylthioimmucillin-H (PDB ID 1Q1G) and DADMe-immucillin-G (PDB ID 3PHC)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PNPH_PLAFA
245
0
26858
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant Y160F/V66I/V73I in complex with immucillin H, sitting drop vapor diffusion method, using 0.2 M magnesium chloride hexahydrate, 0.1 M HEPES at pH 7.5, and 30% (v/v) 2-propanol
analysis of the structures of MTI (PDB ID 1Q1G) and DADMe-I (PDB ID 3PHC) co-crystallized with the protein structure of PfPNP
enzyme in complex with the inhibitor 5'-methylthio-immucillin-H, hanging-drop vapor-diffusion method
-
in complex with phosphate and immucillin-H, sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol monomethyl ether 2000, 100 mM Tris (pH 8.5), and 0.2 M trimethylamine N-oxide dihydrate
-
modeling of the inhibitors 1-((2-pyrrolidine-1-yl)ethyl)uracil and 3-((2-pyrrolidine-1-yl)ethyl)uracil into the active site of the protein, PDB entry 1NW4, by superposition of the uracil ring and the purine ring of Immucillin-H. Both compounds can fit adequately in the active site. In both cases the uracil base is predicted to be oriented in the nucleoside binding pocket by a pi-stacking similar to the purine base of Immucillin-H. The N1 of the uracil base in 1-((2-pyrrolidine-1-yl)ethyl)uracil and the N3 of the uracil base in 3-((2-pyrrolidine-1-yl)ethyl)uracil roughly superimpose with the C4 of Immucillin-H
molecular dynamics simulation in ligand free form and in complex with immucillin and sulfate. The overall structures are stable along the molecular dynamics simulations
-
structures of purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V66I/V73I
the mutant shows increased activity compared to the wild type enzyme
V66I/Y160F
the mutant shows increased activity compared to the wild type enzyme
Y160F
the mutant shows reduced activity compared to the wild type enzyme
Y160F/V66I/V73I
the mutant has a 83fold decrease in turnover number for 5'-methylthioinosine with 2fold increase in Km value compared to the wild type enzyme
additional information
additional information
targeted gene disruption results in loss of enzyme activity in lysate, with normal activity of adenosine deaminase. Mutant parasites show a greater requirement for exogenous purines and a severe growth defect at physiological concentrations of hypoxanthine. The mutant parasites are more sensitive to purine nucelotide phosphorylase inhibitors that bind human purine nucelotide phosphorylase tighter and less sensitive to inhibitor 5'-methylthio-immucillin-H
additional information
-
targeted gene disruption results in loss of enzyme activity in lysate, with normal activity of adenosine deaminase. Mutant parasites show a greater requirement for exogenous purines and a severe growth defect at physiological concentrations of hypoxanthine. The mutant parasites are more sensitive to purine nucelotide phosphorylase inhibitors that bind human purine nucelotide phosphorylase tighter and less sensitive to inhibitor 5'-methylthio-immucillin-H
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
in 50 mM sodium phosphate buffer (pH 7.5), 1 mM EDTA, 1 mM dithiothreitol and 20% (w/v) of various crowding agents like PEG3300, PEG 8000, Dextran 70, sucrose and glycerol
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
Plasmodium falciparum purine nucleoside phosphorylase (PfPNP) can be targeted for antimalarial drug design since its inhibition kills malaria parasites both in vitro and in vivo
drug development
the enzyme is a target for development of anti-malarial drugs
medicine
-
the enzyme inhibitors 8-amino-5'-deoxy-5'-chloroguanosine and 8-amino-9-benzylguanine may have some antimalarial potential by limiting hypoxanthine production in the parasite-infected erythrocyte
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daddona, P.E.; Wiesmann, W.P.; Milhouse, W.; Chern, J.W.; Townsend, L.B.; Hershfield, M.S.; Webster, H.K.
Expression of human malaria parasite purine nucleoside phosphorylase in host enzyme-deficient erythrocyte culture. Enzyme characterization and identification of novel inhibitors
J. Biol. Chem.
261
11667-11673
1986
Homo sapiens, Plasmodium falciparum
Bzowska, A.; Kulikowska, E.; Shugar, D.
Purine nucleoside phosphorylases: properties, functions, and clinical aspects
Pharmacol. Ther.
88
349-425
2000
Acholeplasma laidlawii, Klebsiella aerogenes, Geobacillus stearothermophilus, Bacillus cereus, Cellulomonas sp., Pectobacterium carotovorum, Fasciola hepatica, Klebsiella sp., Micrococcus luteus, Mus musculus, Plasmodium falciparum, Plasmodium lophurae, Proteus vulgaris, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Saccharolobus solfataricus, Trypanosoma brucei, Trypanosoma cruzi, Homo sapiens (P00491), Homo sapiens, Escherichia coli (P0ABP8), Bacillus subtilis (P46354), Bos taurus (P55859), Saccharomyces cerevisiae (Q05788)
Schnick, C.; Robien, M.A.; Brzozowski, A.M.; Dodson, E.J.; Murshudov, G.N.; Anderson, L.; Luft, J.R.; Mehlin, C.; Hol, W.G.; Brannigan, J.A.; Wilkinson, A.J.
Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine
Acta Crystallogr. Sect. D
61
1245-1254
2005
Plasmodium falciparum
Shi, W.; Ting, L.M.; Kicska, G.A.; Lewandowicz, A.; Tyler, P.C.; Evans, G.B.; Furneaux, R.H.; Kim, K.; Almo, S.C.; Schramm, V.L.
Plasmodium falciparum purine nucleoside phosphorylase: crystal structures, immucillin inhibitors, and dual catalytic function
J. Biol. Chem.
279
18103-18106
2004
Plasmodium falciparum, Homo sapiens (P00491), Homo sapiens
Rinaldo-Matthis, A.; Wing, C.; Ghanem, M.; Deng, H.; Wu, P.; Gupta, A.; Tyler, P.C.; Evans, G.B.; Furneaux, R.H.; Almo, S.C.; Wang, C.C.; Schramm, V.L.
Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues
Biochemistry
46
659-668
2007
Trichomonas vaginalis, Homo sapiens (P00491), Homo sapiens, Bos taurus (P55859), Plasmodium falciparum (Q8T9Z7)
Silva, R.G.; Nunes, J.E.; Canduri, F.; Borges, J.C.; Gava, L.M.; Moreno, F.B.; Basso, L.A.; Santos, D.S.
Purine nucleoside phosphorylase: a potential target for the development of drugs to treat T-cell- and apicomplexan parasite-mediated diseases
Curr. Drug Targets
8
413-422
2007
Plasmodium lophurae, Toxoplasma gondii, Homo sapiens (P00491), Homo sapiens, Bos taurus (P55859), Plasmodium falciparum (Q8T9Z7)
Chaudhary, K.; Ting, L.M.; Kim, K.; Roos, D.S.
Toxoplasma gondii purine nucleoside phosphorylase biochemical characterization, inhibitor profiles, and comparison with the Plasmodium falciparum ortholog
J. Biol. Chem.
281
25652-25658
2006
Toxoplasma gondii (Q2HXR2), Toxoplasma gondii, Plasmodium falciparum (Q8T9Z7), Plasmodium falciparum
Taylor, E.A.; Rinaldo-Matthis, A.; Li, L.; Ghanem, M.; Hazleton, K.Z.; Cassera, M.B.; Almo, S.C.; Schramm, V.L.
Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition
Biochemistry
46
12405-12415
2007
Plasmodium falciparum, Anopheles gambiae (A4Q998), Anopheles gambiae, Homo sapiens (P00491), Homo sapiens
Madrid, D.C.; Ting, L.M.; Waller, K.L.; Schramm, V.L.; Kim, K.
Plasmodium falciparum purine nucleoside phosphorylase is critical for viability of malaria parasites
J. Biol. Chem.
283
35899-35907
2008
Plasmodium falciparum (Q8T9Z7), Plasmodium falciparum
Zanchi, F.B.; Caceres, R.A.; Stabeli, R.G.; de Azevedo, W.F.
Molecular dynamics studies of a hexameric purine nucleoside phosphorylase
J. Mol. Model.
16
543-550
2010
Plasmodium falciparum
Ting, L.M.; Gissot, M.; Coppi, A.; Sinnis, P.; Kim, K.
Attenuated Plasmodium yoelii lacking purine nucleoside phosphorylase confer protective immunity
Nat. Med.
14
954-958
2008
Plasmodium falciparum, Plasmodium yoelii
Cui, H.; Ruda, G.F.; Carrero-Lerida, J.; Ruiz-Perez, L.M.; Gilbert, I.H.; Gonzalez-Pacanowska, D.
Exploring new inhibitors of Plasmodium falciparum purine nucleoside phosphorylase
Eur. J. Med. Chem.
45
5140-5149
2010
Plasmodium falciparum (Q8I3X4), Plasmodium falciparum
Donaldson, T.M.; Cassera, M.B.; Ho, M.C.; Zhan, C.; Merino, E.F.; Evans, G.B.; Tyler, P.C.; Almo, S.C.; Schramm, V.L.; Kim, K.
Inhibition and structure of Toxoplasma gondii purine nucleoside phosphorylase
Eukaryot. Cell
13
572-579
2014
Plasmodium falciparum, Toxoplasma gondii (Q2HXR2), Toxoplasma gondii
Suthar, M.K.; Doharey, P.K.; Verma, A.; Saxena, J.K.
Behavior of Plasmodium falciparum purine nucleoside phosphorylase in macromolecular crowded environment
Int. J. Biol. Macromol.
62
657-662
2013
Plasmodium falciparum
Donaldson, T.M.; Ting, L.M.; Zhan, C.; Shi, W.; Zheng, R.; Almo, S.C.; Kim, K.
Structural determinants of the 5-methylthioinosine specificity of Plasmodium purine nucleoside phosphorylase
PLoS ONE
9
e84384
2014
Plasmodium falciparum (Q8T9Z7), Plasmodium falciparum
Wierzchowski, J.; Stachelska-Wierzchowska, A.; Wielgus-Kutrowska, B.; Bzowska, A.
1,N6-ethenoadenine and other fluorescent nucleobase analogs as substrates for purine-nucleoside phosphorylases Spectroscopic and kinetic studies
Curr. Pharm. Des.
23
6948-6966
2017
Bacillus cereus, Pectobacterium carotovorum, Thermus thermophilus, Plasmodium lophurae, Helicobacter pylori (A0A518Y5Z2), Homo sapiens (P00941), Escherichia coli (P0ABP8), Escherichia coli (P45563), Bos taurus (P55859), Cellulomonas sp. (P81989), Plasmodium falciparum (Q8I3X4)
Kagami, L.P.; das Neves, G.M.; Rodrigues, R.P.; da Silva, V.B.; Eifler-Lima, V.L.; Kawano, D.F.
Identification of a novel putative inhibitor of the Plasmodium falciparum purine nucleoside phosphorylase exploring the purine salvage pathway to design new antimalarial drugs
Mol. Divers.
21
677-695
2017
Plasmodium falciparum (Q8I3X4), Plasmodium falciparum
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