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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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Select one or more organisms in this record:
This record set is specific for:
Pyrococcus furiosus
UNIPROT: Q8U2I1
Word Map
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The enzyme appears in selected viruses and cellular organisms
Synonyms
5'-deoxy-5'-methylthioadenosine phosphorylase II, 5'-methythioadenosine phosphorylase, adenine nucleoside phosphorylase, adenosine phosphorylase, AgPNP, ANP, ApMTAP, apPNP, bovPNP, bPNO, 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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PfPNP
281093, 321
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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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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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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
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
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?
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
?
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enzyme is able to reactivate scrambled RNaseA
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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
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28977
6 * 28977, calculated from sequence
29000
6 * 29000, SDS-PAGE
180000
gel filtration
29208
6 * 29208, calculated from sequence
180000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 28977, calculated from sequence; 6 * 29000, SDS-PAGE
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
105
half-life: 69 min
110
Tm-value is 110°C, half-life: 12 min
115
half-life: 5 min
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
three pairs of intrasubunit disulfide bridges play a role in the stability of the enzyme against thermal inactivation
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
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