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Information on EC 2.4.2.1 - purine-nucleoside phosphorylase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.1 purine-nucleoside phosphorylase
IUBMB 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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
pnp, purine nucleoside phosphorylase, pnpase, pfpnp, purine-nucleoside phosphorylase, adenosine phosphorylase, hspnp, hppnp, tvpnp, inosine phosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine phosphorylase
-
-
-
-
Ino-Guo phosphorylase
-
inosine phosphorylase
-
-
-
-
inosine-guanosine phosphorylase
-
-
-
-
nucleotide phosphatase (2.4.2.1)
-
-
-
-
phosphorylase, purine nucleoside
-
-
-
-
PNPase
Pu-NPase
-
-
-
-
PUNP
-
-
-
-
PUNPI
-
-
-
-
PUNPII
-
-
-
-
purine deoxynucleoside phosphorylase
-
-
-
-
purine deoxyribonucleoside phosphorylase
-
-
-
-
purine nucleoside phosphorylase
purine ribonucleoside phosphorylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
purine ribonucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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 hide
9030-21-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-dideoxyinosine + phosphate
hypoxanthine + 2,3-dideoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
?
2'-deoxyguanosine + phosphate
guanine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
2-amino-6-mercapto-7-methylpurine ribonucleoside + phosphate
alpha-D-ribose 1-phosphate + ?
show the reaction diagram
-
-
-
-
?
2-fluoro-2-deoxyadenosine + phosphate
adenine + 2-fluoro-2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
no substrate for wild-type, substrate of double mutant E201Q/N243D
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
?
6-mercaptoguanosine + phosphate
alpha-D-ribose 1-phosphate + 6-mercaptoguanine
show the reaction diagram
-
-
-
-
?
6-mercaptopurine riboside + phosphate
alpha-D-ribose 1-phosphate + 6-mercaptopurine
show the reaction diagram
-
-
-
-
?
6-thioxanthine + alpha-D-ribose 1-phosphate
6-thioxanthosine + phosphate
show the reaction diagram
-
-
-
-
?
7-(beta-D-ribofuranosyl)guanine + alpha-D-ribose 1-phosphate
?
show the reaction diagram
-
-
-
?
7-(beta-D-ribofuranosyl)hypoxanthine + alpha-D-ribose 1-phosphate
?
show the reaction diagram
-
-
-
?
7-methyl-6-thio-guanosine + phosphate
7-methyl-6-thioguanine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
7-methyl-6-thioguanosine + phosphate
7-methyl-6-thioguanine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
7-methyladenosine + phosphate
7-methyladenine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
?
7-methylguanine + alpha-D-ribose 1-phosphate
7-methylguanosine + phosphate
show the reaction diagram
-
-
-
r
7-methylguanosine + phosphate
7-methylguanine + alpha-D-ribose 1-phosphate
show the reaction diagram
7-methylinosine + phosphate
7-methylhypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
?
7-N-methyl-6-thiopurine riboside + phosphate
?
show the reaction diagram
-
-
-
-
?
8-aminoguanine + alpha-D-ribose 1-phosphate
8-aminoguanosine + phosphate
show the reaction diagram
8-azaguanosine + phosphate
8-azaguanine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
adenine + deoxyribose 1-phosphate
deoxyadenosine + phosphate
show the reaction diagram
adenosine + phosphate
adenine + alpha-D-ribose 1-phosphate
show the reaction diagram
deoxyguanosine + phosphate
guanine + alpha-D-deoxyribose 1-phosphate
show the reaction diagram
deoxyinosine + phosphate
hypoxanthine + alpha-D-deoxyribose 1-phosphate
show the reaction diagram
guanine + alpha-D-ribose 1-phosphate
guanosine + phosphate
show the reaction diagram
-
-
-
r
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
show the reaction diagram
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
methylthioinosine + phosphate
methylthiohypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
?
N7-D-ribosyl-2,6-diamino-8-azapurine + phosphate
2,6-diamino-8-azapurine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
nicotinamide riboside + phosphate
nicotinamide + alpha-D-ribose 1-phosphate
show the reaction diagram
purine deoxyribonucleoside + phosphate
purine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
purine ribonucleoside + phosphate
purine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
ribavirin + phosphate
1,2,4-triazole-3-carboxamide + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
xanthosine + arsenate
xanthine + alpha-D-ribose 1-arsenate
show the reaction diagram
-
-
-
-
?
xanthosine + phosphate
alpha-D-ribose 1-phosphate + xanthine
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2'-deoxyguanosine + phosphate
guanine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
7-methylguanine + alpha-D-ribose 1-phosphate
7-methylguanosine + phosphate
show the reaction diagram
-
-
-
r
8-azaguanosine + phosphate
8-azaguanine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
adenosine + phosphate
adenine + alpha-D-ribose 1-phosphate
show the reaction diagram
very low activity
-
-
r
guanine + alpha-D-ribose 1-phosphate
guanosine + phosphate
show the reaction diagram
-
-
-
r
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
show the reaction diagram
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
purine deoxyribonucleoside + phosphate
purine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
purine ribonucleoside + phosphate
purine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+/-)-cis-1,1-difluoro-2-(tetrahydro-3-piranyl)ethylphosphonic acid with (hypoxanthine-9-yl)methyl aglycone
-
multisubstrate analogue inhibitor
(3R,4R)-1-((9-deazahypoxanthin-9-yl)methyl)-4-fluoro-4-hydroxymethyl pyrrolidin-3-ol
-
-
(3S,4R)-4-(guanin-9-yl)-3-hydroxypyrrolidin-1-N-ylcarbonylphosphonic acid
-
competitive. For enzyme from cancer cell lines, Ki values are around 10 to 24 nM
(3S,4S)-1-((9-deazahypoxanthin-9-yl)methyl)-4-fluoro-4-hydroxymethyl pyrrolidin-3-ol
-
-
(S)-3-(guanin-9-yl)pyrrolidin-N-ylcarbonylphosphonic acid
-
competitive. For enzyme from cancer cell lines, Ki values widely vary from 16 to 100 nM
1,5-O-bis(N-benzyloxycarbonylglycyl)-2,3-O-isopropylidene beta-D-riboside
-
1-[2,3-O-isopropylidene-D-ribofuranosyl]-1,4-dihydropyridine-3-carboxamide
-
2-amino-1,5-dihydro-7-[[(2S)-2-(aminomethyl)-1-pyrrolidinyl]-methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 600 nM
2-amino-1,5-dihydro-7-[[(2S)-2-(hydroxymethyl)-1-pyrrolidinyl]methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
acetic acid salt, IC50: 4.0 nM
2-amino-1,5-dihydro-7-[[[2-(hydroxy)ethyl]amino]methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 20 nM
2-Amino-6-methylthiopurine
-
-
2-amino-7-(pyridin-2-ylmethyl)-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
2-amino-7-([[(2R,3S)-1,3,4-trihydroxybutan-2-yl]amino]methyl)-3,5-dihydro-4Hpyrrolo[3,2-d]pyrimidin-4-one
-
i.e. DATMe-immucillin-G
2-amino-7-[4-(benzyloxy)benzyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
2-amino-7-[4-(propan-2-yl)benzyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
1.8fold selectivity for Schistosoma enzyme over human enzyme
2-amino-7-[[(1,3-dihydroxypropan-2-yl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
i.e. SerMe-immucillin-G
2-amino-7-[[(2-hydroxyethyl)(methyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 60 nM
2-amino-7-[[(2R)-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 620 nM
2-amino-7-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 600 nM
2-amino-7-[[(2S,4R)-4-hydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 2 nM
2-amino-7-[[3-(hydroxymethyl)piperidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 0.004 mM
2-amino-7-[[bis(2-hydroxyethyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 5 nM
2-amino-7-[[ethyl(2-hydroxyethyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
IC50: 220 nM
3,5-bis-(4-chlorobenzoyl)-alpha-D-ribose 1-phosphate
-
-
3-carbamoyl-1-[2,3-O-isopropylidene-D-ribofuranosyl]pyridin-1-ium
-
3-[(2R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]-3,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one
6.4fold selectivity for Schistosoma enzyme over human enzyme
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
weak binding inhibitor
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-G
-
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H
5'-chloro-5'-deoxy-8-aminoguanosine
-
-
5'-deoxy-5'-iodo-9-deazainosine
-
5'-deoxy-5'-iodoinosine
-
5'-deoxy-immucillin-H
-
5'-methylthio-immucillin-H
favors inhibition of Plasmodium falciparum purine nucleoside phosphorylase over human enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
6-hydroxy-9-p-aminobenzylpurine
-
-
6-Mercaptopurine
-
-
6-methylthiopurine
-
-
6-Thioxanthine
-
-
6-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
-
7-Deazaguanine
-
7-Deazainosine
-
-
7-deazathioinosine
-
-
7-[(2S,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-2-yl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
-
7-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
i.e. forodesine
7-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]-4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidine-6-carboxylic acid
-
-
7-[[(1,3-dihydroxypropan-2-yl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
i.e. SerMe-immucillin-H. Kd-value 5.2 pM
7-[[(3R,4R)-4-hydroxy-3-(hydroxymethyl)pyrrolidin-2-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
i.e. BCX-4208, mimics the charged ribosyl oxocarbenium ion formed during the transition state
8-amino-3-(2-thienylmethyl)guanine
-
8-amino-5'-deoxy-5'-chloroguanosine
-
-
8-amino-5'-deoxy-5'-iodoguanosine
-
8-Amino-9-benzylguanine
8-aminoguanine
-
-
8-aminoguanosine
-
-
8-aminoquinazolinone
-
8-Bromoadenosine
about 30% inhibition
8-Bromoguanosine
about 30% inhibition
8-dimethylaminoinosine
about 20% inhibition
8-methylaminoinosine
about 30% inhibition
9-(2'-benzyl-5',5'-difluoro-5'-phosphonopentyl)guanine
-
multisubstrate analogue inhibitor
9-(3,4-dihydroxybutyl)guanine
and analogues
9-(3-pyridylmethyl)-9-deaza-guanosine
i.e. peldesine or BCX34
9-(5',5'-difluoro-5'-phosphonobutyl)-9-deazaguanine
-
multisubstrate analogue inhibitor
9-(5',5'-difluoro-5'-phosphonoheptyl)-9-deazaguanine
-
multisubstrate analogue inhibitor
9-(5,5-difluorophosphonopentyl)guanine
-
9-(5-phosphonopentyl)guanine
-
9-benzylguanine
9-deazaguanine
-
multisubstrate analogue inhibitor
acyclovir
adenine
-
-
allopurinol
-
-
alpha-D-ribose 1-phosphate
-
-
apigenin
77.4% inhibition at 0.15 mM, reversible inhibition
baicalein
72% inhibition at 0.15 mM, reversible inhibition
chrysin
5,7-dihydroxyflavone, a natural flavone found in various plant extracts, including blue passionflower, honey and propolis, etc., 38.8% inhibition at 0.15 mM, reversible inhibition
cis-1-((9-deazahypoxanthin-9-yl)methyl)-4-fluoro-4-hydroxymethylpyrrolidin-3-ol
-
-
DADMe-immucillin-G
DADMe-immucillin-H
DATMe-immucillin-H
deoxyinosine
-
-
diphosphate
-
-
Formycin A
an analogue of adenosine
formycin B
forodesine
-
a highly potent, orally active, rationally designed PNP inhibitor, that is active in preclinical studies with malignant cells and clinical utility against T-cell acute lymphoblastic leukemia and cutaneous T-cell lymphoma; a highly potent, orally active, rationally designed PNP inhibitor, use for the management of some B-cell malignancies
forodesine hydrochloride
-
ganciclovir
guanine
guanosine
hypoxanthine
immucillin-A
weak binding inhibitor
immucillin-G
immucillin-H
Inosine
-
-
L-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H
L-immucillin-H
-
N(7)-acycloguanosine
-
N(9)-acycloguanosine
-
N7-acycloguanosine
-
nicotinamide 5-O-glycyl-beta-D-riboside
-
nicotinamide 5-O-L-isoleucyl-beta-D-riboside
-
nicotinamide 5-O-L-leucyl-beta-D-riboside
-
nicotinamide 5-O-L-methionyl-beta-D-riboside
-
nicotinamide 5-O-L-tryptophanyl-beta-D-riboside
-
nicotinamide 5-O-L-tyrosinyl-beta-D-riboside
-
nicotinamide 5-O-L-valyl-beta-D-riboside
-
Oxoallopurinol
-
-
PCMB
-
-
phosphate
quinazolinone
-
reduced nicotinamide 5-O-(N-tert-butyloxycarbonyl-L-isoleucyl)-2,3-O-isopropylidene beta-D-riboside
-
reduced nicotinamide 5-O-(N-tert-butyloxycarbonyl-L-leucyl)-2,3-O-isopropylidene beta-D-riboside
-
reduced nicotinamide 5-O-(N-tert-butyloxycarbonyl-L-methionyl)-2,3-O-isopropylidene beta-D-riboside
-
reduced nicotinamide 5-O-(N-tert-butyloxycarbonyl-L-tyrosinyl)-2,3-O-isopropylidene beta-D-riboside
-
reduced nicotinamide 5-O-(N-tert-butyloxycarbonyl-L-valyl)-2,3-O-isopropylidene beta-D-riboside
-
reduced nicotinamide 5-O-(N-tert-butyloxycarbonylglycyl)-2,3-O-isopropylidene beta-D-riboside
-
reduced nicotinamide 5-O-(N1,Nalpha-bis(tert-butyloxycarbonyl)-L-tryptophanyl)-2,3-O-isopropylidene beta-D-riboside
-
SerMe-immucillin-H
ulodesine
-
xanthine
-
poor inhibitor of phosphorolysis of guanosine
Xanthosine
-
poor inhibitor of phosphorolysis of guanosine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Inosine
-
substrate activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.391 - 14.9
2',3'-dideoxyinosine
0.264
2-fluoro-2'-deoxyadenosine
-
mutant E201Q/N243D
0.167
6-mercaptoguanosine
-
-
0.07
6-mercaptopurine riboside
-
-
0.108
7-(beta-D-ribofuranosyl)guanine
-
1.26
7-(beta-D-ribofuranosyl)hypoxanthine
-
0.358
7-methyl-6-thio-guanosine
-
pH 7.6
9.2 - 39.3
7-methylguanosine
0.37
7-Methylinosine
-
0.012 - 0.08
7-N-methyl-6-thiopurine riboside
0.41
adenine
-
-
0.228
alpha-D-ribose 1-phosphate
-
reaction with guanine
1.8
arsenate
-
-
0.038 - 0.0443
deoxyguanosine
0.066
deoxyinosine
-
-
0.006 - 0.8
guanine
0.012 - 0.092
guanosine
0.01 - 2.3
hypoxanthine
0.022 - 19
Inosine
0.012
Methylthioinosine
pH 7.5, 25°C
0.032 - 91
phosphate
0.38 - 0.425
xanthine
0.58 - 1.6
Xanthosine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 10.5
2',3'-dideoxyinosine
0.155
2-fluoro-2'-deoxyadenosine
-
mutant E201Q/N243D
6.23 - 73.1
7-methylguanosine
48
guanine
recombinant erythrocyte enzyme
2 - 60
guanosine
0.5 - 130
hypoxanthine
0.01 - 56
Inosine
0.2
Methylthioinosine
pH 7.5, 25°C
0.09 - 76
phosphate
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 23.14
2',3'-dideoxyinosine
568
2-fluoro-2'-deoxyadenosine
-
mutant E201Q/N243D
240 - 5860
7-methylguanosine
150 - 1020
guanosine
0.00014 - 1400
Inosine
115.15
phosphate
pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000072
(+/-)-cis-1,1-difluoro-2-(tetrahydro-3-piranyl)ethylphosphonic acid with (hypoxanthine-9-yl)methyl aglycone
-
erythrocyte enzyme, pH 7.0, 25°C
0.00000182
(3R,4R)-1-((9-deazahypoxanthin-9-yl)methyl)-4-fluoro-4-hydroxymethyl pyrrolidin-3-ol
-
overall dissociation constant
0.01
(3S,4R)-4-(guanin-9-yl)-3-hydroxypyrrolidin-1-N-ylcarbonylphosphonic acid
-
recombinant enzyme, pH 7.5, temperature not specified in the publication
0.000000032
(3S,4S)-1-((9-deazahypoxanthin-9-yl)methyl)-4-fluoro-4-hydroxymethyl pyrrolidin-3-ol
-
overall dissociation constant
0.02
(S)-3-(guanin-9-yl)pyrrolidin-N-ylcarbonylphosphonic acid
-
recombinant enzyme, pH 7.5, temperature not specified in the publication
0.000306
2-amino-1,5-dihydro-7-[[(2S)-2-(aminomethyl)-1-pyrrolidinyl]-methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
37°C, pH 7.0
0.000002
2-amino-1,5-dihydro-7-[[(2S)-2-(hydroxymethyl)-1-pyrrolidinyl]methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
37°C, pH 7.0, acetic acid salt
0.0000102
2-amino-1,5-dihydro-7-[[[2-(hydroxy)ethyl]amino]methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
37°C, pH 7.0
0.3
2-Amino-6-methylthiopurine
-
-
0.0000000034
2-amino-7-([[(2R,3S)-1,3,4-trihydroxybutan-2-yl]amino]methyl)-3,5-dihydro-4Hpyrrolo[3,2-d]pyrimidin-4-one
-
-
0.0000000021
2-amino-7-[[(1,3-dihydroxypropan-2-yl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
-
0.0000306
2-amino-7-[[(2-hydroxyethyl)(methyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
0.0003163
2-amino-7-[[(2R)-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
0.0003061
2-amino-7-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
0.000001
2-amino-7-[[(2S,4R)-4-hydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
0.0000018
2-amino-7-[[3-(hydroxymethyl)piperidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
0.0000025
2-amino-7-[[bis(2-hydroxyethyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
0.0001122
2-amino-7-[[ethyl(2-hydroxyethyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
0.0000000107 - 0.00000095
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H
0.0004
5'-chloro-5'-deoxy-8-aminoguanosine
-
-
0.00018
5'-deoxy-5'-iodo-9-deazainosine
-
0.018
5'-deoxy-5'-iodoinosine
-
0.0000000077 - 0.000000198
5'-deoxy-immucillin-H
0.203
6-hydroxy-9-p-aminobenzylpurine
-
-
0.073
6-Mercaptopurine
-
-
0.13
6-methylthiopurine
-
-
1.1
6-Thioxanthine
-
-
0.2
7-Deazaguanine
pH 7.6, 25°C
0.33
7-Deazainosine
-
-
0.000000016
7-[[(3R,4R)-4-hydroxy-3-(hydroxymethyl)pyrrolidin-2-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
-
0.0033
8-amino-5'-deoxy-5'-iodoguanosine
-
0.0002
8-Amino-9-benzylguanine
0.0002
8-aminoguanine
-
-
0.007 - 0.017
8-aminoguanosine
0.0000076
9-(2'-benzyl-5',5'-difluoro-5'-phosphonopentyl)guanine
-
erythrocyte enzyme, pH 7.0, 25°C
0.0000135
9-(3-pyridylmethyl)-9-deaza-guanosine
pH and temperature not specified in the publication
0.0000081
9-(5',5'-difluoro-5'-phosphonobutyl)-9-deazaguanine
-
erythrocyte enzyme, pH 7.0, 25°C
0.0000053
9-(5',5'-difluoro-5'-phosphonoheptyl)-9-deazaguanine
-
erythrocyte enzyme, pH 7.0, 25°C
0.0000056
9-deazaguanine
-
erythrocyte enzyme, pH 7.0, 25°C
0.09
acyclovir
-
6.6
adenine
-
-
0.97
allopurinol
-
-
0.000000066
cis-1-((9-deazahypoxanthin-9-yl)methyl)-4-fluoro-4-hydroxymethylpyrrolidin-3-ol
-
overall dissociation constant
0.000000034 - 0.000000121
DADMe-immucillin-G
0.000000009 - 0.00000035
DADMe-immucillin-H
0.000000009
DATMe-immucillin-H
pH and temperature not specified in the publication
1.5
deoxyinosine
-
-
0.33
diphosphate
-
-
0.1 - 0.5
formycin B
0.004 - 0.0125
guanine
0.01
guanosine
0.007 - 0.01
hypoxanthine
0.000000133 - 0.000000175
immucillin-G
0.000000011 - 0.000001
immucillin-H
0.26
Inosine
-
-
0.00000038
L-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H
-
slow-onset binding constant
0.005
N(7)-acycloguanosine
-
0.014
N(9)-acycloguanosine
-
0.81
Oxoallopurinol
-
-
4.4 - 26
phosphate
0.323
quinazolinone
-
0.000000005
SerMe-immucillin-H
pH and temperature not specified in the publication
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
2-amino-1,5-dihydro-7-[[(2S)-2-(aminomethyl)-1-pyrrolidinyl]-methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 600 nM
0.000004
2-amino-1,5-dihydro-7-[[(2S)-2-(hydroxymethyl)-1-pyrrolidinyl]methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
acetic acid salt, IC50: 4.0 nM
0.00002
2-amino-1,5-dihydro-7-[[[2-(hydroxy)ethyl]amino]methyl]-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 20 nM
0.000023
2-amino-7-(pyridin-2-ylmethyl)-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
pH 7.4, 25°C
0.0003
2-amino-7-[4-(benzyloxy)benzyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
pH 7.4, 25°C
0.00027
2-amino-7-[4-(propan-2-yl)benzyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
pH 7.4, 25°C
0.00006
2-amino-7-[[(2-hydroxyethyl)(methyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 60 nM
0.00062
2-amino-7-[[(2R)-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 620 nM
0.0006
2-amino-7-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 600 nM
0.000002
2-amino-7-[[(2S,4R)-4-hydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 2 nM
0.004
2-amino-7-[[3-(hydroxymethyl)piperidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 0.004 mM
0.000005
2-amino-7-[[bis(2-hydroxyethyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 5 nM
0.00022
2-amino-7-[[ethyl(2-hydroxyethyl)amino]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
Homo sapiens
IC50: 220 nM
0.372
3,5-bis-(4-chlorobenzoyl)-alpha-D-ribose 1-phosphate
Homo sapiens
-
pH 7.6, 37°C
0.3
3-[(2R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]-3,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one
Homo sapiens
pH 7.4, 25°C
0.0609
apigenin
Homo sapiens
pH 7.4, 37°C
0.0894
baicalein
Homo sapiens
pH 7.4, 37°C
0.213
chrysin
Homo sapiens
pH 7.4, 37°C
additional information
additional information
Homo sapiens
-
IC50 values of compounds 6-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one, 7-[(2S,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-2-yl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one, and 7-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]-4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidine-6-carboxylic acid are in the range of 100-300 nM
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12
-
presence of 100 mM phosphate, pH 7.0
139
-
presence of 50 mM phosphate, pH 7.0
20
-
presence of 50 mM phosphate, pH 7.0
41
-
presence of 50 mM phosphate, pH 7.0
46
-
presence of 100 mM phosphate, pH 7.0
47
-
presence of 100 mM phosphate, pH 7.0
53.3
-
-
55
-
reaction with guanosine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
-
reaction with xanthine or xanthosine
6.6
assay at
7 - 8
-
reaction with guanine, guanosine, hypoxanthine and inosine
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
25 - 37
assay at
30
assay at
37
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
peripheral blood mononuclear cell
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LACC1_HUMAN
430
0
47780
Swiss-Prot
other Location (Reliability: 2)
PNPH_HUMAN
289
0
32118
Swiss-Prot
other Location (Reliability: 1)
Q05DJ2_HUMAN
242
0
26791
TrEMBL
other Location (Reliability: 2)
V9HWH6_HUMAN
289
0
32118
TrEMBL
other Location (Reliability: 1)
J3QSB7_HUMAN
242
0
26777
TrEMBL
other Location (Reliability: 2)
A0A140CZL6_HUMAN
233
0
25613
TrEMBL
other Location (Reliability: 2)
Q9P1G4_HUMAN
96
0
10303
TrEMBL
other Location (Reliability: 2)
A0A140CZL5_HUMAN
233
0
25630
TrEMBL
other Location (Reliability: 2)
Q8N7G1_HUMAN
293
0
32551
TrEMBL
other Location (Reliability: 1)
G3V5M2_HUMAN
221
0
24479
TrEMBL
Mitochondrion (Reliability: 2)
G3V393_HUMAN
61
0
6913
TrEMBL
Secretory Pathway (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29700
-
3 * 29700, SDS-PAGE
30000
31600
-
3 * 31600, SDS-PAGE
32000
-
2 * 32000, SDS-PAGE
67000
-
equilibrium sedimentation, gel filtration, amino acid analysis
80000 - 92000
-
gel filtration, equilibrium sedimentation
81000
-
gel filtration
91000
-
equilibrium sedimentation
93800
-
disc gel electrophoresis
94000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30000, SDS-PAGE
homohexamer
-
homotrimer
monomer
trimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallization of L-immucillin-H and 4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H with the enzyme and phosphate. The structures with L-immucillin-H and 4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H are solved to 2.9 A and 2.1 A resolution, respectively
conformational states in complex with transition state analogues Immucillin-H and DATMe-Immucillin-H. The (purine nucelotide phosphorylase)3(PO4)3 ImmH-complex is more compact by sedimentation rate than the other complexes. Purine nucelotide phosphorylase protein conformation of dynamic motion correlates more closely with entropy of binding than with affinity. Catalytically active turnover with saturated substrate sites causes less change in peptide amide deuterium exchange and sedimentation rates than binding of transition state analogues. DATMe-Immucilin-H more closely mimics the transition of human PNP than does Immucilin-H and achieves strong binding interactions at the catalytic site while causing relatively modest alterations of the protein dynamic motion
crystals for X-ray analysis are obtained by vapor-diffusion equilibration of droplets hanging from siliconized coverslips inverted on Linbro plates
-
hanging drop vapour diffusion. Crystallographic structure of human PNP in complex with guanosine (at 2.80 A resolution), 3'-deoxyguanosine (at 2.86 A resolution) and 8-azaguanine (at 2.85 A resolution)
HsPNP/4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-H/SO4 crystal complexes are prepared by hanging-drop vapor diffusion, HsPNP/immucillin-H/PO4 crystal complexes are prepared by sitting-drop vapor diffusion
in complex with 2-mercapto-4(3H)-quinazolinone at 2.7 A resolution, application to predict ligand positions obtained in docking simulations
in complex with 7-deazaguanine, to 2.75 A resolution. Two intermolecular hydrogen bonds involve the residues Glu201 and Asn243
in complex with transition-state analogues immucillin-H, DADMe-immucillin-H, DATMe-immucillin-H, and immucillin-H, to 2.4 A to 2.5 A resolution. Inhibitor binding sites of purine nucelotide phosphorylase are near the C-terminal region of the 6-stranded beta-sheet. The purine base binding region consists primarily of hydrophobic residues including Phe200, Val217, Met219, Val245, and Val260. Purine base interactions also include the polar residues Glu201 and Asn243 as hydrogen bond acceptors from the NH1 and NH7 groups of 9-deazahypoxanthine. Asn243 also donates hydrogen bonds to O6 of the deazapurine, except in the case of immucillin-H. Features of tight binding are ion-pair formation between bound phosphate or its mimic and inhibitor cation, leaving-group interactions to N1, O6, and N7 of 9-deazahypoxanthine, interaction between phosphate and inhibitor hydroxyl groups, and His257 interacting with the 5'-hydroxyl group
mutant E201Q/N243D in complex with prodrug 2-fluoro-2'-deoxyadenosine and with 2-fluoroadenine. The overall fold of the mutant is nearly identical to the wild type enzyme. The residues Gln201 and Asp243 introduced by the mutation form hydrogen bond contacts with 2-fluoro-2'-deoxyadenosine that result in its binding and catalysis. Comparison of complexes suggest that the side chains of Gln201 and Asp243 as well as the purine base rotate during catalysis possibly facilitating cleavage of the glycosidic bond
recombinant enzyme in complex with 7-methyl-6-thio-guanosine
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A117T
-
mutation leading to purine-nucleoside phosphorylase deficiency, occuring in two sisters
E201Q/N243D
F159G
mutant displays a strong increase in KM and modest decrease in kcat
F159Y
site-directed mutagenesis, pre-steadystate chemistry is reduced 32fold in mutant F159Y PNP. Pre-steady-state chemistry compares heavy and light molecular weight wild-type and mutant F159Y PNPs and finds a normal heavy-enzyme isotope effect of 1.31 for wild-type PNP and an inverse effect of 0.75 for F159Y mutant PNP. Increased isotopic mass in F159Y PNP causes more efficient transition state formation. Most heavy enzymes demonstrate normal heavy-enzyme isotope effects, and F159Y PNP is a rare example of an inverse effect
F200G
mutant displays a strong increase in KM and modest decrease in kcat
G51S
-
the mutant possesses wild type phosphorylase activity levels toward inosine and ribavirin
H257D
kcat/Km for inosine is 1460fold lower than wild-type value, greatly decreased affinity for Immucillin-H
H257F
kcat/Km for inosine is 68fold lower than wild-type value, greatly decreased affinity for Immucillin-H
H257G
kcat/Km for inosine is 610fold lower than wild-type value, greatly decreased affinity for Immucillin-H
H86A
-
10-25fold reduction in catalytic activity
K22E/H104R
L22E/H104R
-
mutation of human toward bovine purine nucleoside phosphorylase. Mutant is similar to human purine nucleoside phosphorylase in steady-state kinetic properties. Inhibitor DADMe-immucillin-G is an excellent mimic of the transition states for both human purine nucleoside phosphorylase and the mutant with a preference for the mutant. Thermodynamic parameters establish the mutant to be catalytically more efficient than the parent enzyme and reveal differences in the entropic component of catalysis
N243A
-
100fold decrease in turnover-number compared to wild-type enzyme
N243D
Q89A
-
10-25fold reduction in catalytic activity
Y88A
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88C
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88D
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88E
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88F
engineering of human enzyme to accept 2',3'-dideoxyinosine as substrate. Mutant displays 9-fold improvement in kcat and greater than 2-fold reduction in KM of 2',3'-dideoxyinosine
Y88H
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88I
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88K
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88L
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88M
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88N
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88Q
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88R
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88S
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88T
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88V
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
Y88W
mutation introduced to render enzyme susceptible to substrate 2',3'-dideoxyinosine
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 10
-
5 min, stable
489651
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57
-
15 min, 50% inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
moderatly stable to X-rays
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing of the enzyme in presence of dithiothreitol results in greater loss of activity than in the absence of a sulfhydryl reagent
-
489676
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% loss of activity after 2 weeks
-
20°C, room temperature, stable for several days in concentrated solution, 1% in 0.02% sodium azide
-
4°C or frozen, stable for long periods of time
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Talon column chromatography
-
partial
-
recombinant
wild-type and recombinant mutant enzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
expression of site-directed mutants in Escherichia coli
-
trans-activator of transcription-mediated long-term intracellular delivery of purine nucleoside phosphorylase corrects its deficiency in mice
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
drug development
differences in specificity between homotrimeric (including human enzyme) and homohexameric PNPs, including various pathogenic organisms, make them interesting potential drug targets
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Agarwal, R.P.; Parks, R.E.
Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties
J. Biol. Chem.
244
644-647
1969
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Parks, R.E.; Agarwal, R.P.
Purine nucleoside phosphorylase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
483-514
1972
Klebsiella aerogenes, Aeromonas hydrophila, Brevibacillus brevis, Bacillus cereus, Bacillus subtilis, Bacillus licheniformis, Bacterium cadaveris, Bos taurus, Canis lupus familiaris, Gallus gallus, Columba livia, Clavibacter michiganensis subsp. sepedonicus, Oryctolagus cuniculus, Escherichia coli, Equus caballus, Pectobacterium carotovorum, Felis catus, Homo sapiens, Lactobacillus leichmannii, Leucisus rusticus, Macaca mulatta, Micrococcus luteus, Papio hamadryas, Proteus vulgaris, Shewanella putrefaciens, Rattus norvegicus, salmon, Salmonella enterica subsp. enterica serovar Enteritidis, Sus scrofa
-
Manually annotated by BRENDA team
Cook, W.J.; Ealick, S.E.; Bugg, C.E.; Stoeckler, J.D.; Parks, R.E.
Crystallization and preliminary X-ray investigation of human erythrocytic purine nucleoside phosphorylase
J. Biol. Chem.
256
4079-4080
1981
Homo sapiens
Manually annotated by BRENDA team
Lewis, A.S.; Lowy, B.A.
Human erythrocyte purine nucleoside phosphorylase: molecular weight and physical properties. A Theorell-Chance catalytic mechanism
J. Biol. Chem.
254
9927-9932
1979
Homo sapiens
Manually annotated by BRENDA team
Osborne, W.R.A.
Human red cell purine nucleoside phosphorylase. Purification by biospecific affinity chromatography and physical properties
J. Biol. Chem.
255
7089-7092
1980
Homo sapiens
Manually annotated by BRENDA team
Stoeckler, J.D.; Agarwal, R.P.; Agarwal, K.C.; Parks, R.E.
Purine nucleoside phosphorylase from human erythrocytes
Methods Enzymol.
51
530-538
1978
Homo sapiens
Manually annotated by BRENDA team
Stoeckler, J.D.; Agarwal, R.P.; Agarwal, K.C.; Schmid, K.; Parks, R.E.
Purine nucleoside phosphorylase from human erythrocytes: physiocochemical properties of the crystalline enzyme
Biochemistry
17
278-283
1978
Homo sapiens
Manually annotated by BRENDA team
Zannis, V.; Doyle, D.; Martin, D.W.
Purification and characterization of human erythrocyte purine nucleoside phosphorylase and its subunits
J. Biol. Chem.
253
504-510
1978
Homo sapiens
Manually annotated by BRENDA team
Bzowska, A.; Kulikowska, E.; Shugar, D.
Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin
Z. Naturforsch. C
45c
59-70
1990
Bos taurus, Escherichia coli, Homo sapiens
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Erion, M.D.; Takabayashi, K.; Smith, H.B.; Kessi, J.; Wagner, S.; Hoenger, S.; Shames, S.L.; Ealick, S.E.
Purine nucleoside phosphorylase. 1. Structure-function Studies
Biochemistry
36
11725-11734
1997
Homo sapiens
Manually annotated by BRENDA team
Stoychev, G.; Kierdaszuk, B.; Shugar, D.
Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems
Eur. J. Biochem.
269
4048-4057
2002
Homo sapiens, Bos taurus (P55859)
Manually annotated by BRENDA team
Montgomery, J.A.
Purine nucleoside phosphorylase: a target for drug design
Med. Res. Rev.
13
209-228
1993
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Silva, R.G.; Pereira, J.H.; Canduri, F.; de Azevedo, W.F., Jr.; Basso, L.A.; Santos, D.S.
Kinetics and crystal structure of human purine nucleoside phosphorylase in complex with 7-methyl-6-thio-guanosine
Arch. Biochem. Biophys.
442
49-58
2005
Homo sapiens
Manually annotated by BRENDA team
Canduri, F.; Fadel, V.; Basso, L.A.; Palma, M.S.; Santos, D.S.; de Azevedo, W.F., Jr.
New catalytic mechanism for human purine nucleoside phosphorylase
Biochem. Biophys. Res. Commun.
327
646-649
2005
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Silva, R.G.; Carvalho, L.P.; Oliveira, J.S.; Pinto, C.A.; Mendes, M.A.; Palma, M.S.; Basso, L.A.; Santos, D.S.
Cloning, overexpression, and purification of functional human purine nucleoside phosphorylase
Protein Expr. Purif.
27
158-164
2003
Homo sapiens
Manually annotated by BRENDA team
Canduri, F.; Silva, R.G.; Marangoni dos Santos, D.; Palma, M.S.; Basso, L.A.; Santos, D.S.; Filgueira de Azevedo, W.J.
Structure of human PNP complexed with ligands
Acta Crystallogr. Sect. D
D61
856-862
2005
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Murkin, A.S.; Birck, M.R.; Rinaldo-Matthis, A.; Shi, W.; Taylor, E.A.; Almo, S.C.; Schramm, V.L.
Neighboring group participation in the transition state of human purine nucleoside phosphorylase
Biochemistry
46
5038-5049
2007
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Toro, A.; Grunebaum, E.
TAT-mediated intracellular delivery of purine nucleoside phosphorylase corrects its deficiency in mice
J. Clin. Invest.
116
2717-2726
2006
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Semeraro, T.; Lossani, A.; Botta, M.; Ghiron, C.; Alvarez, R.; Manetti, F.; Mugnaini, C.; Valensin, S.; Focher, F.; Corelli, F.
Simplified analogues of immucillin-G retain potent human purine nucleoside phosphorylase inhibitory activity
J. Med. Chem.
49
6037-6045
2006
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Nunez, S.; Wing, C.; Antoniou, D.; Schramm, V.L.; Schwartz, S.D.
Insight into catalytically relevant correlated motions in human purine nucleoside phosphorylase
J. Phys. Chem. A
110
463-472
2006
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Saen-Oon, S.; Ghanem, M.; Schramm, V.L.; Schwartz, S.D.
Remote mutations and active site dynamics correlate with catalytic properties of purine nucleoside phosphorylase
Biophys. J.
94
4078-4088
2008
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Rinaldo-Matthis, A.; Murkin, A.S.; Ramagopal, U.A.; Clinch, K.; Mee, S.P.; Evans, G.B.; Tyler, P.C.; Furneaux, R.H.; Almo, S.C.; Schramm, V.L.
L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase
J. Am. Chem. Soc.
130
842-844
2008
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Mason, J.M.; Murkin, A.S.; Li, L.; Schramm, V.L.; Gainsford, G.J.; Skelton, B.W.
A beta-fluoroamine inhibitor of purine nucleoside phosphorylase
J. Med. Chem.
51
5880-5884
2008
Homo sapiens
Manually annotated by BRENDA team
Furman, R.R.; Hoelzer, D.
Purine nucleoside phosphorylase inhibition as a novel therapeutic approach for B-cell lymphoid malignancies
Semin. Oncol.
34
S29-S34
2007
Homo sapiens
Manually annotated by BRENDA team
Timmers, L.F.; Caceres, R.A.; Vivan, A.L.; Gava, L.M.; Dias, R.; Ducati, R.G.; Basso, L.A.; Santos, D.S.; de Azevedo, W.F.
Structural studies of human purine nucleoside phosphorylase: towards a new specific empirical scoring function
Arch. Biochem. Biophys.
479
28-38
2008
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Todorova, N.A.; Schwarz, F.P.
Effect of the phosphate substrate on drug-inhibitor binding to human purine nucleoside phosphorylase
Arch. Biochem. Biophys.
480
122-131
2008
Homo sapiens
Manually annotated by BRENDA team
Ghanem, M.; Li, L.; Wing, C.; Schramm, V.L.
Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase
Biochemistry
47
2559-2564
2008
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Luo, M.; Li, L.; Schramm, V.L.
Remote mutations alter transition-state structure of human purine nucleoside phosphorylase
Biochemistry
47
2565-2576
2008
Homo sapiens
Manually annotated by BRENDA team
Li, L.; Luo, M.; Ghanem, M.; Taylor, E.A.; Schramm, V.L.
Second-sphere amino acids contribute to transition-state structure in bovine purine nucleoside phosphorylase
Biochemistry
47
2577-2583
2008
Homo sapiens (P00491), Homo sapiens, Bos taurus (P55859), Bos taurus
Manually annotated by BRENDA team
Edwards, A.A.; Mason, J.M.; Clinch, K.; Tyler, P.C.; Evans, G.B.; Schramm, V.L.
Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase
Biochemistry
48
5226-5238
2009
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Edwards, A.A.; Tipton, J.D.; Brenowitz, M.D.; Emmett, M.R.; Marshall, A.G.; Evans, G.B.; Tyler, P.C.; Schramm, V.L.
Conformational States of human purine nucleoside phosphorylase at rest, at work, and with transition state analogues
Biochemistry
49
2058-2067
2010
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Kamath, V.P.; Xue, J.; Juarez-Brambila, J.J.; Morris, C.B.; Ganorkar, R.; Morris, P.E.
Synthesis of analogs of forodesine HCl, a human purine nucleoside phosphorylase inhibitor-Part I
Bioorg. Med. Chem. Lett.
19
2624-2626
2009
Homo sapiens
Manually annotated by BRENDA team
Castilho, M.S.; Postigo, M.P.; Pereira, H.M.; Oliva, G.; Andricopulo, A.D.
Structural basis for selective inhibition of purine nucleoside phosphorylase from Schistosoma mansoni: kinetic and structural studies
Bioorg. Med. Chem.
18
1421-1427
2010
Schistosoma mansoni, Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Cao, Y.; Wang, J.; Xu, Y.; Li, G.
Sensing purine nucleoside phosphorylase activity by using silver nanoparticles
Biosens. Bioelectron.
25
1032-1036
2010
Homo sapiens
Manually annotated by BRENDA team
Glavas-Obrovac, L.; Suver, M.; Hikishima, S.; Hashimoto, M.; Yokomatsu, T.; Magnowska, L.; Bzowska, A.
Antiproliferative activity of purine nucleoside phosphorylase multisubstrate analogue inhibitors containing difluoromethylene phosphonic acid against leukaemia and lymphoma cells
Chem. Biol. Drug Des.
75
392-399
2010
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Kamath, V.P.; Juarez-Brambila, J.J.; Morris, P.E.
Synthesis of labeled BCX-4208, a potent inhibitor of purine nucleoside phosphorylase
Drug Test. Anal.
1
125-127
2009
Homo sapiens
Manually annotated by BRENDA team
Aytekin, C.; Dogu, F.; Tanir, G.; Guloglu, D.; Santisteban, I.; Hershfield, M.S.; Ikinciogullari, A.
Purine nucleoside phosphorylase deficiency with fatal course in two sisters
Eur. J. Pediatr.
169
311-314
2010
Homo sapiens
Manually annotated by BRENDA team
Afshar, S.; Olafsen, T.; Wu, A.; Morrison, S.
Characterization of an engineered human purine nucleoside phosphorylase fused to an anti-her2/neu single chain Fv for use in ADEPT
J. Exp. Clin. Cancer Res.
28
147
2009
Homo sapiens
Manually annotated by BRENDA team
Liao, P.; Toro, A.; Min, W.; Lee, S.; Roifman, C.M.; Grunebaum, E.
Lentivirus gene therapy for purine nucleoside phosphorylase deficiency
J. Gene Med.
10
1282-1293
2008
Homo sapiens
Manually annotated by BRENDA team
Clinch, K.; Evans, G.B.; Froehlich, R.F.; Furneaux, R.H.; Kelly, P.M.; Legentil, L.; Murkin, A.S.; Li, L.; Schramm, V.L.; Tyler, P.C.; Woolhouse, A.D.
Third-generation immucillins: syntheses and bioactivities of acyclic immucillin inhibitors of human purine nucleoside phosphorylase
J. Med. Chem.
52
1126-1143
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Caceres, R.A.; Timmers, L.F.; Pauli, I.; Gava, L.M.; Ducati, R.G.; Basso, L.A.; Santos, D.S.; de Azevedo, W.F.
Crystal structure and molecular dynamics studies of human purine nucleoside phosphorylase complexed with 7-deazaguanine
J. Struct. Biol.
169
379-388
2010
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Ho, M.C.; Shi, W.; Rinaldo-Matthis, A.; Tyler, P.C.; Evans, G.B.; Clinch, K.; Almo, S.C.; Schramm, V.L.
Four generations of transition-state analogues for human purine nucleoside phosphorylase
Proc. Natl. Acad. Sci. USA
107
4805-4812
2010
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Afshar, S.; Sawaya, M.R.; Morrison, S.L.
Structure of a mutant human purine nucleoside phosphorylase with the prodrug, 2-fluoro-2-deoxyadenosine and the cytotoxic drug, 2-fluoroadenine
Protein Sci.
18
1107-1114
2009
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Vande Voorde, J.; Quintiliani, M.; McGuigan, C.; Liekens, S.; Balzarini, J.
Inhibition of pyrimidine and purine nucleoside phosphorylases by a 3,5-dichlorobenzoyl-substituted 2-deoxy-D-ribose-1-phosphate derivative
Biochem. Pharmacol.
83
1358-1363
2012
Homo sapiens, Mycoplasma hyorhinis
Manually annotated by BRENDA team
Rejman, D.; Panova, N.; Klener, P.; Maswabi, B.; Pohl, R.; Rosenberg, I.
N-phosphonocarbonylpyrrolidine derivatives of guanine: a new class of bi-substrate inhibitors of human purine nucleoside phosphorylase
J. Med. Chem.
55
1612-1621
2012
Homo sapiens
Manually annotated by BRENDA team
Nannemann, D.; Kaufmann, K.; Meiler, J.; Bachmann, B.
Design and directed evolution of a dideoxy purine nucleoside phosphorylase
Protein Eng. Des. Sel.
23
607-616
2010
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Qi, Y.; Li, Y.; Bao, J.J.
Development of a capillary electrophoresis method for analyzing adenosine deaminase and purine nucleoside phosphorylase and its application in inhibitor screening
Anal. Biochem.
506
31-44
2016
Homo sapiens
Manually annotated by BRENDA team
Isaksen, G.V.; Hopmann, K.H.; Aqvist, J.; Brandsdal, B.O.
Computer simulations reveal substrate specificity of glycosidic bond cleavage in native and mutant human purine nucleoside phosphorylase
Biochemistry
55
2153-2162
2016
Homo sapiens
Manually annotated by BRENDA team
Furihata, T.; Kishida, S.; Sugiura, H.; Kamiichi, A.; Iikura, M.; Chiba, K.
Functional analysis of purine nucleoside phosphorylase as a key enzyme in ribavirin metabolism
Drug Metab. Pharmacokinet.
29
211-214
2014
Homo sapiens
Manually annotated by BRENDA team
Giuliani, P.; Zuccarini, M.; Buccella, S.; Rossini, M.; D'Alimonte, I.; Ciccarelli, R.; Marzo, M.; Marzo, A.; Di Iorio, P.; Caciagli, F.
Development of a new HPLC method using fluorescence detection without derivatization for determining purine nucleoside phosphorylase activity in human plasma
J. Chromatogr. B
1009-1010
114-121
2016
Homo sapiens
Manually annotated by BRENDA team
Suarez, J.; Schramm, V.L.
Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase
Proc. Natl. Acad. Sci. USA
112
11247-11251
2015
Homo sapiens
Manually annotated by BRENDA team
Roca, M.; Moliner, V.; Tunon, I.
Origin of enzymatic kinetic isotope effects in human purine nucleoside phosphorylase
ACS Catal.
8
815-827
2018
Homo sapiens (P00491)
-
Manually annotated by BRENDA team
Cattaneo, G.; Ubiali, D.; Calleri, E.; Rabuffetti, M.; Hoefner, G.C.; Wanner, K.T.; De Moraes, M.C.; Martinelli, L.K.B.; Santos, D.S.; Speranza, G.; Massolini, G.
Development, validation and application of a 96-well enzymatic assay based on LC-ESI-MS/MS quantification for the screening of selective inhibitors against Mycobacterium tuberculosis purine nucleoside phosphorylase
Anal. Chim. Acta
943
89-97
2016
Mycobacterium tuberculosis, Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Isaksen, G.V.; Aqvist, J.; Brandsdal, B.O.
Thermodynamics of the purine nucleoside phosphorylase reaction revealed by computer simulations
Biochemistry
56
306-312
2017
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Wen, Q.H.; Wang, L.H.; Zeng, X.A.; Niu, D.B.; Wang, M.S.
Hydroxyl-related differences for three dietary flavonoids as inhibitors of human purine nucleoside phosphorylase
Int. J. Biol. Macromol.
118
588-598
2018
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Stachelska-Wierzchowska, A.; Wierzchowski, J.; Bzowska, A.; Wielgus-Kutrowska, B.
Site-selective ribosylation of fluorescent nucleobase analogs using purine-nucleoside phosphorylase as a catalyst effects of point mutations
Molecules
21
44
2016
Homo sapiens (P00491), Homo sapiens, Escherichia coli (P0ABP8), Escherichia coli, Bos taurus (P55859)
Manually annotated by BRENDA team
Hayat, F.; Migaud, M.E.
Nicotinamide riboside-amino acid conjugates that are stable to purine nucleoside phosphorylase
Org. Biomol. Chem.
18
2877-2885
2020
Homo sapiens (P00491)
Manually annotated by BRENDA team
Harijan, R.K.; Zoi, I.; Antoniou, D.; Schwartz, S.D.; Schramm, V.L.
Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase
Proc. Natl. Acad. Sci. USA
114
6456-6461
2017
Homo sapiens (P00491), Homo sapiens
Manually annotated by BRENDA team
Jackson, E.K.; Gillespie, D.G.; Cheng, D.; Mi, Z.; Menshikova, E.V.
Characterization of the N6-etheno-bridge method to assess extracellular metabolism of adenine nucleotides detection of a possible role for purine nucleoside phosphorylase in adenosine metabolism
Purinergic Signal.
16
187-211
2020
Homo sapiens (P00491), Rattus norvegicus (P85973), Rattus norvegicus Wistar-Kyoto (P85973)
Manually annotated by BRENDA team