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Information on EC 2.4.2.1 - purine-nucleoside phosphorylase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U2I1

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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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This record set is specific for:
Pyrococcus furiosus
UNIPROT: Q8U2I1
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
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
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inosine phosphorylase
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inosine-guanosine phosphorylase
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nucleotide phosphatase (2.4.2.1)
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phosphorylase, purine nucleoside
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PNPase
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Pu-NPase
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PUNP
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PUNPI
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-
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PUNPII
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purine deoxynucleoside phosphorylase
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purine deoxyribonucleoside phosphorylase
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purine nucleoside phosphorylase
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purine ribonucleoside phosphorylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine + phosphate
adenine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
show the reaction diagram
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-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
show the reaction diagram
absolute specificity for inosine and guanosine
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-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
absolute specificity for inosine and guanosine
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-
?
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
adenosine + phosphate
adenine + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
show the reaction diagram
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-
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r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.122
guanosine
80°C
0.322
Inosine
80°C, pH 7.4
0.122
guanosine
80°C
0.322
Inosine
80°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28.05
guanosine
80°C
84.19
Inosine
80°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0179
80°C, production of hypoxanthine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75 - 133
75°C: about 55% of maximal activity, 133°C: about 50% of maximal activity
additional information
thermophilic signature of the enzyme, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
gel filtration
28977
6 * 28977, calculated from sequence
29000
6 * 29000, SDS-PAGE
180000
gel filtration
29208
6 * 29208, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
hexamer
6 * 29208, calculated from sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C254S/C256S
reduced thermodynamic and kinetic stability of the mutant with respect to the wild-type PfPNP
C254S/C256S
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120
Tm-value in presence of 100 mM phosphate
100
4 h, stable, wild-type enzyme. Mutant enzyme C254S/C256S shows 38% residual activity after 4 h incubation
102
Tm-value for mutant enzyme C254S/C256S
105
half-life: 69 min for wild-type enzyme, 35.5 min for mutant enzyme C254S/C256S
110
half-life: 12 min, Tm-value 110°C increases to 120°C in the presence of 100 mM phosphate, wild-type enzyme
115
half-life: 5 min, wild-type enzyme
120
Tm-value 110°C increases to 120°C in the presence of 100 mM phosphate, wild-type enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
limited proteolysis indicated that the only proteolytic cleavage site is localized in the C-terminal region
phosphate is able to increase the already high stability of PfPNP toward SDS
remarkable SDS-resistance, enzyme remains fully active after 30 min in 2% SDS at 50°C and retains 60% residual activity after 5 min at 90°C
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SDS
2%, the enzyme remains fully active after 30 min incubation at 50°C and still retains 60% residual activity after 5 min incubation at 90°C. Phosphate is able to increase the already high stability of PfPNP toward the detergent
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the CXC motif is necessary to obtain complete renaturation from the unfolded state. After denaturation using 6 M guadinium HCl, wild-type is able to achieve a recovery of catalytic activity of 90%. Sequence NH2-RRCGCKD-COOH acts as in vitro catalyst of oxidative protein folding
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cacciapuoti, G.; Gorassini, S.; Mazzeo, M.F.; Siciliano, R.A.; Carbone, V.; Zappia, V.; Porcelli, M.
Biochemical and structural characterization of mammalian-like purine nucleoside phosphorylase from the Archaeon Pyrococcus furiosus
FEBS J.
274
2482-2495
2007
Pyrococcus furiosus, Pyrococcus furiosus (Q8U2I1)
Manually annotated by BRENDA team
Cacciapuoti, G.; Peluso, I.; Fuccio, F.; Porcelli, M.
Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding
FEBS J.
276
5799-5805
2009
Pyrococcus furiosus
Manually annotated by BRENDA team
Kamel, S.; Thiele, I.; Neubauer, P.; Wagner, A.
Thermophilic nucleoside phosphorylases their properties, characteristics and applications
Biochim. Biophys. Acta
1868
140304
2020
Parageobacillus thermoglucosidasius, Deinococcus geothermalis, Aeropyrum pernix (A0A401H9D3), Geobacillus stearothermophilus (P77834), Geobacillus stearothermophilus (P77835), Thermus thermophilus (Q72IR2), Thermus thermophilus (Q72L69), Pyrococcus furiosus (Q8U2I1), Pyrococcus furiosus ATCC 43587 (Q8U2I1), Thermus thermophilus DSM 7039 (Q72IR2), Thermus thermophilus DSM 7039 (Q72L69), Pyrococcus furiosus Vc1 (Q8U2I1), Deinococcus geothermalis DSM 11300, Deinococcus geothermalis AG-3a, Parageobacillus thermoglucosidasius 11955, Pyrococcus furiosus JCM 8422 (Q8U2I1), Thermus thermophilus ATCC BAA-163 (Q72IR2), Thermus thermophilus ATCC BAA-163 (Q72L69)
Manually annotated by BRENDA team