We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adenosine phosphorylase
-
-
-
-
inosine phosphorylase
-
-
-
-
inosine-guanosine phosphorylase
-
-
-
-
nucleotide phosphatase (2.4.2.1)
-
-
-
-
phosphorylase, purine nucleoside
-
-
-
-
purine deoxynucleoside phosphorylase
-
-
-
-
purine deoxyribonucleoside phosphorylase
-
-
-
-
purine nucleoside phosphorylase
-
-
-
-
purine ribonucleoside phosphorylase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pentosyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adenosine + phosphate
adenine + alpha-D-ribose 1-phosphate
-
-
-
r
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
absolute specificity for inosine and guanosine
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
absolute specificity for inosine and guanosine
-
-
?
additional information
?
-
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
r
additional information
?
-
thermophilic PNPs and PyNPs accept nucleosides with arabinose, C2'-fluororibose and C2'-fluoroarabinose as the sugar moiety. Substrate spectrum of thermostable nucleoside phosphorylases, overview
-
-
-
additional information
?
-
-
enzyme is able to reactivate scrambled RNaseA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adenosine + phosphate
adenine + alpha-D-ribose 1-phosphate
-
-
-
r
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.322
Inosine
80°C, pH 7.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0179
80°C, production of hypoxanthine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
75 - 133
75°C: about 55% of maximal activity, 133°C: about 50% of maximal activity
additional information
thermophilic signature of the enzyme, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
28977
6 * 28977, calculated from sequence
29000
6 * 29000, SDS-PAGE
29208
6 * 29208, calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hexamer
6 * 29208, calculated from sequence
hexamer
6 * 28977, calculated from sequence
hexamer
6 * 29000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C254S/C256S
reduced thermodynamic and kinetic stability of the mutant with respect to the wild-type PfPNP
C254S/C256S
Tm-value is 8°C lower than Tm-value of wild-type enzyme
C254S/C256S
-
after denaturation using 6 M guadinium HCl, mutant achieves a recovery of catalytic activity of 46%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
105
half-life: 69 min
110
Tm-value is 110°C, half-life: 12 min
115
half-life: 5 min
additional information
-
three pairs of intrasubunit disulfide bridges play a role in the stability of the enzyme against thermal inactivation
additional information
three pairs of intrasubunit disulfide bridges play a role in the stability of the enzyme against thermal inactivation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli
expressed in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
brenda
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
brenda
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)
brenda