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2',3'-cAMP + H2O
?
-
-
-
-
?
3'-dTMP + H2O
?
Tequatrovirus T4
-
-
-
-
?
3'-phopsho-5'-hydroxy-DNA
?
3'-phospho-5'-hydroxy-ATTCGTGTGAGAAAACCCAACCCGCCCTACCCAAAAGTCAGATGA + H2O
?
Tequatrovirus T4
-
the enzyme mediates 5'-phosphorylation of ATTCGTGTGAGAAAACCCAACCCGCCCTACCCAAAAGTCAGATGA
-
-
?
3'-phospho-5'-hydroxy-DNA
?
3'-phospho-5'-hydroxy-DNA + H2O
?
3'-phospho-5'-hydroxy-poly(dT,dA) + H2O
3'-hydroxy-5'-phospho-poly(dT,dA)
-
poly(dT,dA) with a 3' phosphate and and 5' OH group, preparation of substrate, presence of ATP
-
?
3'-phospho-5'-hydroxy-RNA + H2O
?
Tequatrovirus T4
-
-
-
-
?
3'-phosphopolynucleotide + H2O
polynucleotide + phosphate
a RNA 2',3'-cyclic phosphate end + H2O
a RNA 3'-phosphate + phosphate
Tequatrovirus T4
-
the enzyme also has RNA 2'-phosphatase activity
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
-
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
p-nitrophenyl phosphate + phosphate
-
-
-
-
?
bleomycin-damaged DNA + H2O
?
-
-
?
d(TTTAATCAATTGCGACCCp) + H2O
phosphate + d(TTTAATCAATTGCGACCC)
-
reaction with the end-healing domain Rnl1-(394-694), that consists of a proximal 5'-kinase module with an essential P-loop motif (404GSGKS408) and a distal 3'-phosphatase module with an essential acylphosphatase motif (560DLDGT564)
-
-
?
DNA with 3'-phosphate ends + H2O
DNA + phosphate
-
-
-
?
DNA with 5'-hydroxyl ends + ATP
DNA with 5'-phosphate ends + ADP
-
-
-
?
DNA with single-strand breaks + H2O
?
-
-
?
dTMP + H2O
thymidine + phosphate
FAM-5'-TAGAGAGAGAGAGAGAGAGAGAGCGCA CCTAAAGGGTGCG-phospho-3' + H2O
FAM-5'-TAGAGAGAGAGAGAGAGAGAGAGCGCA CCTAAAGGGTGCG-hydroxyl-3' + phosphate
Tequatrovirus T4
-
the primer probe can be dephosphorylated by the enzyme into a 3'-hydroxyl end
-
-
?
H2O2-damaged DNA + H2O
?
-
-
?
oligodeoxyadenylate 3'-phosphate + H2O
oligodeoxyadenylate + phosphate
-
-
-
?
p-nitrophenyl phenylphosphonate + H2O
?
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
phosphorylated DNA ends + H2O
?
phosphorylated DNA-ends + H2O
DNA-ends + phosphate
thymidine 3'-monophosphate + H2O
thymidine + phosphate
-
-
-
?
additional information
?
-
3'-phopsho-5'-hydroxy-DNA
?
role in repair of DNA strand breaks caused by oxidative damage
-
-
?
3'-phopsho-5'-hydroxy-DNA
?
-
the enzyme is capable of converting a 3'-phosphate/5'-OH strand of nicked DNA, which is unreparable by DNA ligase into a reparable 3'-OH/5'-phosphate nick in double stranded DNA
-
-
?
3'-phospho-5'-hydroxy-DNA
?
-
-
-
-
?
3'-phospho-5'-hydroxy-DNA
?
Tequatrovirus T4
-
-
-
-
?
3'-phospho-5'-hydroxy-DNA + H2O
?
-
-
-
-
?
3'-phospho-5'-hydroxy-DNA + H2O
?
Tequatrovirus T4
-
-
-
-
?
3'-phosphopolynucleotide + H2O
polynucleotide + phosphate
-
-
-
-
?
3'-phosphopolynucleotide + H2O
polynucleotide + phosphate
-
-
-
-
?
3'-phosphopolynucleotide + H2O
polynucleotide + phosphate
-
-
-
-
?
dsDNA + H2O
?
-
preferred substrate
-
?
dTMP + H2O
thymidine + phosphate
Kostyavirus CJW1
-
-
-
?
dTMP + H2O
thymidine + phosphate
Omegavirus omega
-
-
-
?
phosphorylated DNA ends + H2O
?
Kostyavirus CJW1
-
-
-
-
?
phosphorylated DNA ends + H2O
?
Omegavirus omega
-
-
-
-
?
phosphorylated DNA-ends + H2O
DNA-ends + phosphate
Kostyavirus CJW1
-
-
-
r
phosphorylated DNA-ends + H2O
DNA-ends + phosphate
Omegavirus omega
-
-
-
r
pTp + H2O
pT + phosphate
-
-
-
?
pTp + H2O
pT + phosphate
-
-
-
-
?
additional information
?
-
-
not active towards dimethyl-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine
-
-
?
additional information
?
-
-
structure of the human PNKP FHA domain bound to a doubly phosphorylated phosphopeptide derived from XRCC1, overview
-
-
?
additional information
?
-
-
the enzyme acts on mitochondrial DNA and interacts with the mitochondrial proteins, overview
-
-
?
additional information
?
-
-
polynucleotide kinase/phosphatase is a bifunctional enzyme that can phosphorylate the 5'-OH termini and dephosphorylate the 3'-phosphate termini of DNA. Recombinant GFP-tagged PfPNKP dephosphorylates single-stranded substrates or double-stranded substrates with a short 3-single-stranded overhang, but not double-stranded substrates that mimicked single-strand breaks
-
-
?
additional information
?
-
-
polynucleotide kinase/phosphatase is a bifunctional enzyme that can phosphorylate the 5'-OH termini and dephosphorylate the 3'-phosphate termini of DNA. 3'-Phosphatase activity is detected, and PfPNKP dephosphorylates single-stranded substrates or double-stranded substrates with a short 3'-single-stranded overhang, but not double-stranded substrates that mimick single-strand breaks. But the recombinant PfPNKP does not reveal 5'-kinase activity
-
-
?
additional information
?
-
-
recombinant enzyme shows no activity with micrococcal nuclease digested DNA, nicked DNA, GC and AT rich 20-, 10-, 8-, 5-base oligonucleotides, and polyA that contain 5'-hydroxyl termini
-
-
?
additional information
?
-
-
repair of endogenously created 3-phosphate, involved in Rad1/Rad10 salvage pathway
-
?
additional information
?
-
removes 3-phosphates from nicks and single-nucleotide gaps with equal efficiency, inactive on single-stranded oligonucleotides
-
?
additional information
?
-
-
removes 3-phosphates from nicks and single-nucleotide gaps with equal efficiency, inactive on single-stranded oligonucleotides
-
?
additional information
?
-
acts in the repair of damaged DNA
-
?
additional information
?
-
-
acts in the repair of damaged DNA
-
?
additional information
?
-
Tequatrovirus T4
-
polynucleotide kinase/phosphatase is a bifunctional enzyme with 5'-kinase and 3'-phosphatase activities which can generate 5'-phosphate and 3'-hydroxyl groups at damaged DNA termini, thus permitting subsequent repair proteins to replace missing nucleotides and rejoin broken strands
-
-
?
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Adenoma
Polynucleotide kinase 3' phosphatase variant, dietary variables and risk of adenoma recurrence in the Polyp Prevention Trial.
Apraxias
A new XRCC1-containing complex and its role in cellular survival of methyl methanesulfonate treatment.
Apraxias
A Novel Homozygous Variant in the Fork-Head-Associated Domain of Polynucleotide Kinase Phosphatase in a Patient Affected by Late-Onset Ataxia With Oculomotor Apraxia Type 4.
Apraxias
From congenital microcephaly to adult onset cerebellar ataxia: Distinct and overlapping phenotypes in patients with PNKP gene mutations.
Apraxias
The RIR motif in the scaffold protein XRCC1 mediates a low-affinity interaction with polynucleotide kinase/phosphatase (PNKP) during DNA single-strand break repair.
Ataxia
A new XRCC1-containing complex and its role in cellular survival of methyl methanesulfonate treatment.
Ataxia
A Novel Homozygous Variant in the Fork-Head-Associated Domain of Polynucleotide Kinase Phosphatase in a Patient Affected by Late-Onset Ataxia With Oculomotor Apraxia Type 4.
Ataxia
From congenital microcephaly to adult onset cerebellar ataxia: Distinct and overlapping phenotypes in patients with PNKP gene mutations.
Ataxia
Pathological mutations in PNKP trigger defects in DNA single-strand break repair but not DNA double-strand break repair.
Ataxia
The RIR motif in the scaffold protein XRCC1 mediates a low-affinity interaction with polynucleotide kinase/phosphatase (PNKP) during DNA single-strand break repair.
Brain Diseases
Genes of early-onset epileptic encephalopathies: from genotype to phenotype.
Breast Neoplasms
Elevated PI3K signaling drives multiple breast cancer subtypes.
Charcot-Marie-Tooth Disease
Pathological mutations in PNKP trigger defects in DNA single-strand break repair but not DNA double-strand break repair.
Charcot-Marie-Tooth Disease
The polynucleotide kinase 3'-phosphatase gene (PNKP) is involved in Charcot-Marie-Tooth disease (CMT2B2) previously related to MED25.
Colonic Neoplasms
Synthetic Lethal Targeting of PTEN-Deficient Cancer Cells Using Selective Disruption of Polynucleotide Kinase/Phosphatase.
Colorectal Neoplasms
A synthetically lethal nanomedicine delivering novel inhibitors of polynucleotide kinase 3'-phosphatase (PNKP) for targeted therapy of PTEN-deficient colorectal cancer.
Decompression Sickness
A nick-sensing DNA 3'-repair enzyme from Arabidopsis.
Endometrial Neoplasms
Direct identification of PTEN phosphorylation sites.
Genetic Diseases, Inborn
Impact of PNKP mutations associated with microcephaly, seizures and developmental delay on enzyme activity and DNA strand break repair.
Glioblastoma
Direct identification of PTEN phosphorylation sites.
Leukemia
Genetic screening for synthetic lethal partners of polynucleotide kinase/phosphatase: potential for targeting SHP-1 depleted cancers.
Leukemia, Myeloid
The human polynucleotide kinase/phosphatase (hPNKP) inhibitor A12B4C3 radiosensitizes human myeloid leukemia cells to Auger electron-emitting anti-CD123 (111)In-NLS-7G3 radioimmunoconjugates.
Lymphoma
Genetic screening for synthetic lethal partners of polynucleotide kinase/phosphatase: potential for targeting SHP-1 depleted cancers.
Machado-Joseph Disease
The Role of the Mammalian DNA End-processing Enzyme Polynucleotide Kinase 3'-Phosphatase in Spinocerebellar Ataxia Type 3 Pathogenesis.
Melanoma
Direct identification of PTEN phosphorylation sites.
Microcephaly
A Novel Homozygous Variant in the Fork-Head-Associated Domain of Polynucleotide Kinase Phosphatase in a Patient Affected by Late-Onset Ataxia With Oculomotor Apraxia Type 4.
Microcephaly
From congenital microcephaly to adult onset cerebellar ataxia: Distinct and overlapping phenotypes in patients with PNKP gene mutations.
Microcephaly
Impact of PNKP mutations associated with microcephaly, seizures and developmental delay on enzyme activity and DNA strand break repair.
Microcephaly
Microcephalic primordial dwarfism in an Emirati patient with PNKP mutation.
Microcephaly
Pathological mutations in PNKP trigger defects in DNA single-strand break repair but not DNA double-strand break repair.
Microcephaly
Polynucleotide kinase-phosphatase (PNKP) mutations and neurologic disease.
Microcephaly
The RIR motif in the scaffold protein XRCC1 mediates a low-affinity interaction with polynucleotide kinase/phosphatase (PNKP) during DNA single-strand break repair.
Neoplasms
A synthetically lethal nanomedicine delivering novel inhibitors of polynucleotide kinase 3'-phosphatase (PNKP) for targeted therapy of PTEN-deficient colorectal cancer.
Neoplasms
Correlation between synaptogenesis and the PTEN phosphatase expression in dendrites during postnatal brain development.
Neoplasms
Direct identification of PTEN phosphorylation sites.
Neoplasms
Elevated PI3K signaling drives multiple breast cancer subtypes.
Neoplasms
Genetic screening for synthetic lethal partners of polynucleotide kinase/phosphatase: potential for targeting SHP-1 depleted cancers.
Neoplasms
Monitoring regulation of DNA repair activities of cultured cells in-gel using the comet assay.
Neoplasms
Synthetic Lethal Targeting of PTEN-Deficient Cancer Cells Using Selective Disruption of Polynucleotide Kinase/Phosphatase.
Neoplasms
The lipogenic LXR-SREBF1 signaling pathway controls cancer cell DNA repair and apoptosis and is a vulnerable point of malignant tumors for cancer therapy.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Why high cholesterol levels help hematological malignancies: role of nuclear lipid microdomains.
Prostatic Neoplasms
Genetic screening for synthetic lethal partners of polynucleotide kinase/phosphatase: potential for targeting SHP-1 depleted cancers.
Seizures
From congenital microcephaly to adult onset cerebellar ataxia: Distinct and overlapping phenotypes in patients with PNKP gene mutations.
Seizures
Impact of PNKP mutations associated with microcephaly, seizures and developmental delay on enzyme activity and DNA strand break repair.
Seizures
Microcephalic primordial dwarfism in an Emirati patient with PNKP mutation.
Seizures
Pathological mutations in PNKP trigger defects in DNA single-strand break repair but not DNA double-strand break repair.
Seizures
The RIR motif in the scaffold protein XRCC1 mediates a low-affinity interaction with polynucleotide kinase/phosphatase (PNKP) during DNA single-strand break repair.
Spinocerebellar Ataxias
The Role of the Mammalian DNA End-processing Enzyme Polynucleotide Kinase 3'-Phosphatase in Spinocerebellar Ataxia Type 3 Pathogenesis.
Werner Syndrome
Biochemical mechanisms of chromosomal translocations resulting from DNA double-strand breaks.
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0.0000179
3'-phospho-5'-hydroxy-DNA
-
at pH 7.5 and 37°C
0.548
3'-phosphopolynucleotide
-
-
1.6 - 88
bis-p-nitrophenyl phosphate
0.0039
DNA with 5'-hydroxyl ends
-
-
67
p-Nitrophenyl phenylphosphonate
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
1 - 75
p-nitrophenyl phosphate
3.9
2',3'-cAMP
-
mutant enzyme H376D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
4.7
2',3'-cAMP
-
mutant enzyme H376N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
6.6
2',3'-cAMP
-
mutant enzyme D236N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
7.8
2',3'-cAMP
-
mutant enzyme D236A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
18
2',3'-cAMP
-
mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
18
2',3'-cAMP
-
mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
18
2',3'-cAMP
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
20
2',3'-cAMP
-
mutant enzyme H189D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
24
2',3'-cAMP
-
mutant enzyme H323Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
28
2',3'-cAMP
-
mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
29
2',3'-cAMP
-
mutant enzyme H189A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
31
2',3'-cAMP
-
mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
32
2',3'-cAMP
-
mutant enzyme H323A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
60
2',3'-cAMP
-
mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
62
2',3'-cAMP
-
mutant enzyme D233E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
77
2',3'-cAMP
-
mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
100
2',3'-cAMP
-
mutant enzyme D392A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
100
2',3'-cAMP
-
mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
1.6
bis-p-nitrophenyl phosphate
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
2.2
bis-p-nitrophenyl phosphate
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
3.4
bis-p-nitrophenyl phosphate
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
3.6
bis-p-nitrophenyl phosphate
-
mutant enzyme H189D, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
5
bis-p-nitrophenyl phosphate
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
5
bis-p-nitrophenyl phosphate
-
mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
5
bis-p-nitrophenyl phosphate
-
mutant enzyme H376D, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2
6.3
bis-p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
6.6
bis-p-nitrophenyl phosphate
-
mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2
7.2
bis-p-nitrophenyl phosphate
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
7.4
bis-p-nitrophenyl phosphate
-
mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
9.6
bis-p-nitrophenyl phosphate
-
mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
11
bis-p-nitrophenyl phosphate
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
12
bis-p-nitrophenyl phosphate
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
12
bis-p-nitrophenyl phosphate
-
mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
18
bis-p-nitrophenyl phosphate
-
mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
18
bis-p-nitrophenyl phosphate
-
mutant enzyme R237Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
24
bis-p-nitrophenyl phosphate
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
26
bis-p-nitrophenyl phosphate
-
mutant enzyme H189Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
38
bis-p-nitrophenyl phosphate
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
58
bis-p-nitrophenyl phosphate
-
mutant enzyme H189E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
88
bis-p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
1
p-nitrophenyl phosphate
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
1.3
p-nitrophenyl phosphate
-
mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
4.9
p-nitrophenyl phosphate
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
5
p-nitrophenyl phosphate
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
6.6
p-nitrophenyl phosphate
-
mutant enzyme D236E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
12
p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
13
p-nitrophenyl phosphate
-
mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
75
p-nitrophenyl phosphate
-
mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.42
3'-phospho-5'-hydroxy-DNA
-
at pH 7.5 and 37°C
0.26 - 253.3
bis-p-nitrophenyl phosphate
27.83
p-Nitrophenyl phenylphosphonate
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
1.88 - 146.7
p-nitrophenyl phosphate
0.003 - 0.0043
phosphorylated DNA ends
-
additional information
2',3'-cAMP
-
mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
0.04 - 1.97
2',3'-cAMP
-
mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
0.04 - 1.97
2',3'-cAMP
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
0.833
2',3'-cAMP
-
mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
0.97
2',3'-cAMP
-
mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
1.1
2',3'-cAMP
-
mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
1.45
2',3'-cAMP
-
mutant enzyme H189A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
1.67
2',3'-cAMP
-
mutant enzyme D392A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
3.2
2',3'-cAMP
-
mutant enzyme H376D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
3.25
2',3'-cAMP
-
mutant enzyme D233E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
3.5
2',3'-cAMP
-
mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
4.53
2',3'-cAMP
-
mutant enzyme D236A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
5.13
2',3'-cAMP
-
mutant enzyme H376N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
5.77
2',3'-cAMP
-
mutant enzyme D236N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
6.03
2',3'-cAMP
-
mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
6.5
2',3'-cAMP
-
mutant enzyme H323Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
8.1
2',3'-cAMP
-
mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
8.55
2',3'-cAMP
-
mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
8.93
2',3'-cAMP
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
9.1
2',3'-cAMP
-
mutant enzyme H323A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
15.97
2',3'-cAMP
-
mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
17.17
2',3'-cAMP
-
mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
18.67
2',3'-cAMP
-
mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
20.17
2',3'-cAMP
-
mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
26.17
2',3'-cAMP
-
mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
34.33
2',3'-cAMP
-
mutant enzyme H189D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C
0.26
bis-p-nitrophenyl phosphate
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
0.52
bis-p-nitrophenyl phosphate
-
mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
0.92
bis-p-nitrophenyl phosphate
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
1.1
bis-p-nitrophenyl phosphate
-
mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
1.23
bis-p-nitrophenyl phosphate
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
1.7
bis-p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
2.13
bis-p-nitrophenyl phosphate
-
mutant enzyme H376D, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2
2.53
bis-p-nitrophenyl phosphate
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
3 - 6
bis-p-nitrophenyl phosphate
-
mutant enzyme H189D, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
3.13
bis-p-nitrophenyl phosphate
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0),0.5 mM MnCl2
3.33
bis-p-nitrophenyl phosphate
-
mutant enzyme H189Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
3.63
bis-p-nitrophenyl phosphate
-
mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
3.72
bis-p-nitrophenyl phosphate
-
mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
4.05
bis-p-nitrophenyl phosphate
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0),0.5 mM MnCl2
8.8
bis-p-nitrophenyl phosphate
-
mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
9.33
bis-p-nitrophenyl phosphate
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
12
bis-p-nitrophenyl phosphate
-
mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
13.77
bis-p-nitrophenyl phosphate
-
mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
16.9
bis-p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
18
bis-p-nitrophenyl phosphate
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
19.33
bis-p-nitrophenyl phosphate
-
mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
23.17
bis-p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
33
bis-p-nitrophenyl phosphate
-
mutant enzyme R237Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
43.5
bis-p-nitrophenyl phosphate
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
52.33
bis-p-nitrophenyl phosphate
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
65.83
bis-p-nitrophenyl phosphate
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
117.5
bis-p-nitrophenyl phosphate
-
mutant enzyme H189E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
253.3
bis-p-nitrophenyl phosphate
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
0.58
dTMP
Kostyavirus CJW1
-
-
0.63
dTMP
Omegavirus omega
-
-
6.08
dTMP
Omegavirus omega
-
-
6.08
dTMP
Kostyavirus CJW1
-
-
1.88
p-nitrophenyl phosphate
-
mutant enzyme D236E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
2.5
p-nitrophenyl phosphate
-
mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
3.42
p-nitrophenyl phosphate
-
mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
5.25
p-nitrophenyl phosphate
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
9.58
p-nitrophenyl phosphate
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
15
p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
30.83
p-nitrophenyl phosphate
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
38.33
p-nitrophenyl phosphate
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
146.7
p-nitrophenyl phosphate
-
mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2
0.003
phosphorylated DNA ends
Omegavirus omega
-
-
-
0.0043
phosphorylated DNA ends
Kostyavirus CJW1
-
-
-
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evolution
-
differences between PfPNKP and the other PNKP Walker A box/P loops: the sequence of the P-loop consensus sequence is hGxPGxGKSTh (h is hydrophobic, x is any amino acid), whereas the sequence of the P-loop of PfPNKP is IGPPGCGKTFL. Second, the difference between glutamic acid at position 330 of PfPNKP
malfunction
-
mutations result in severe neurological disease
malfunction
-
mutations that lead to alterations in PNKP, similar to mutations in genes encoding other strand break repair proteins, are associated with a severe autosomal recessive neurological disorder
malfunction
-
pnk1pku70 and pnk1rhp51 double mutants are more sensitive to gamma-radiation than single mutants. Mutation pnk1apn2 is synthetically lethal. But the nth1pnk1apn2 and tdp1pnk1apn2 triple mutants are viable, implying that single-strand breaks with 3'-blocked termini produced by Nth1 and Tdp1 contribute to synthetic lethality
metabolism
-
Pnk1 and Apn2 may function in parallel pathways essential for the repair of endogenous DNA damage
metabolism
-
aprataxin polynucleotide kinase/phosphatase-like factor (APLF) facilitates nonhomologous end joining (NHEJ) and associates with the core NHEJ components XRCC4-DNA ligase IV and Ku. The APLF-Ku interaction is functionally important in DNA repair and may be important for APLF stability
metabolism
-
interaction between XRCC1 and polynucleotide kinase 3'-phosphatase is critical for the retention of XRCC1 at DNA damage sites and DNA damage repair
physiological function
Tequatrovirus T4
-
DNA 3'-phosphatases play a unique role in repair of double strand breaks induced by DNA damaging agents, such as ionizing radioation or oxidative stress
physiological function
-
polynucleotide kinase/phosphatase is a bifunctional enzyme that can phosphorylate the 5'-OH termini and dephosphorylate the 3'-phosphate termini of DNA. It is a DNA repair enzyme involved in the processing of strand break termini, which permits subsequent repair proteins to replace missing nucleotides and rejoin broken strands. PfPNKP may not be involved in single-strand break repair, since alternative terminal processing mechanisms can substitute for PfPNKP, and that PfPNKP DNA repair actions may be confined to overhanging termini of double-strand breaks
physiological function
-
polynucleotide kinase/phosphatase serves a crucial role in the repair of DNA strand breaks by catalyzing the restoration of 5'-phosphate and 3'-hydroxyl termini. It is involved in single-strand break repair and participates in several DNA repair pathways through interactions with other DNA repair proteins, notably XRCC1 and XRCC4, regulation and enzyme recruitment, overview. Physiological importance of PNKP in maintaining the genomic stability of normal tissues, particularly developing neural cells, as well as enhancing the resistance of cancer cells to genotoxic therapeutic agents. The enzyme also performs base excision and double-strand break repair, overview
physiological function
-
polynucleotide kinase/phosphatase serves a crucial role in the repair of DNA strand breaks by catalyzing the restoration of 5'-phosphate and 3'-hydroxyl termini. It is involved in single-strand break repair and participates in several DNA repair pathways through interactions with other DNA repair proteins, notably XRCC1 and XRCC4, regulation and enzyme recruitment, overview. Physiological importance of PNKP in maintaining the genomic stability of normal tissues, particularly developing neural cells, as well as enhancing the resistance of cancer cells to genotoxic therapeutic agents. The enzyme also performs base excision and double-strand break repair, overview
physiological function
-
the enzyme is involved in repair of DNA single and double strand breaks following exposure of cells to ionizing radiation
physiological function
-
PfPNKP may not be involved in single-strand break repair, since alternative terminal processing mechanisms can substitute for PfPNKP, PfPNKP DNA repair actions may be confined to overhanging termini of double-strand breaks
physiological function
-
Pnk1 phosphatase activity, but not kinase activity, is required for DNA repair. Pnk1's primary role is independent of either homologous recombination or non-homologous end joining mechanisms. Construction of a model where Tdp1 and Pnk1 act in concert in an Apn2-independent base excision repair pathway to repair 3'-blocked termini produced by Nth1
physiological function
-
the mitochondrial enzyme polynucleotide kinase/phosphatase is required in mitochondrial DNA repair, overview
physiological function
Tequatrovirus T4
-
this enzyme plays an important role in nucleic acid metabolism and DNA repairing during strand interruption
physiological function
mice with PNKP inactivation in neural progenitors manifest neurodevelopmental abnormalities and postnatal death. The phenotype involves defective base excision repair and nonhomologous end-joining. Mice homozygous for the T424GfsX48 frame-shift allele are lethal embryonically, and attenuated PNKP levels akin to microcephaly with seizures syndrome show general neurodevelopmental defects. Directed postnatal neural inactivation of PNKP affects specific subpopulations including oligodendrocytes
physiological function
-
PNKP stably associates with ataxin-3. Purified wild-type ataxin-3 stimulates, and the mutant form specifically inhibits, PNKP's 3'-phosphatase activity in vitro. ATXN3-deficient cells also show decreased PNKP activity
physiological function
the phosphatase domain binds 3'-phosphorylated single-stranded DNAs in a manner that is highly dependent on the presence of the 3'-phosphate. Double-stranded substrate binding is not as dependent on the 3'-phosphate. The predicted loss of energy due to base pair disruption upon binding of the phosphatase active site is likely balanced by favorable interactions between the liberated complementary strand and PNKP. The surrounding surfaces of the active site cleft are important in binding to double-stranded substrates
physiological function
transgenic mice conditionally expressing the pathological form of human ataxin-3, a polyglutamine repeat-containing protein mutated in spinocerebellar ataxia type 3, also show decreased 3'-phosphatase activity of PNKP, mostly in the deep cerebellar nuclei
additional information
-
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP FHA domain to phosphorylated motifs on XRCC1 and XRCC4, overview
additional information
-
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP FHA domain to phosphorylated motifs on XRCC1 and XRCC4, overview. The crystal structure of murine PNKP shows that the two catalytic active sites are positioned on the same side of the protein
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D233E
-
decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
D392A
-
7-10% as active as wild type Pnkp
H189Q
-
decreased activity compared to the wild type enzyme
H264N
-
increased activity compared to the wild type enzyme
H264Q
-
decreased activity compared to the wild type enzyme
H323A
-
60% of wild type activity
H323Q
-
decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
H376A
-
7-10% as active as wild type Pnkp
N263A
-
7-10% as active as wild type Pnkp
D169A
Kostyavirus CJW1
-
half of wild type 5-kinase activity, almost complete loss of 3-phosphatase activity
K15A
Kostyavirus CJW1
-
no 5-kinase activity, reduced 3-phosphates activity
D170A
mutation of the first aspartate of the conserved phosphatase motif, catalytically inactive but structurally intact protein
D175A
Omegavirus omega
-
reduced 5-kinase activity, no 3-phosphatase activity
K16A
Omegavirus omega
-
retains 5-kinase activity, reduced 3-phosphatase activity
D206A
-
some remaining activity
D206E
-
severely impaired activity
D218A
-
some remaining activity
D218E
-
no enzymic activity
D35A
-
no enzymic activity
D35E
-
some remaining activity
D35N
-
no enzymic activity
D37A
-
some remaining activity
D37E
-
severely impaired activity
K170A
-
no enzymic activity
S88A
-
severely impaired activity
T39A
-
some remaining activity
D165A
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D165E
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D165N
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D167A
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D167E
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D176A
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D176K
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D187A
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
D187E
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
D187N
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
D213A
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D213K
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D254A
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D254E
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D254N
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D277A
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
D277E
Tequatrovirus T4
-
retains 93% activity of the wild type enzyme
D277N
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
D278A
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D278E
Tequatrovirus T4
-
partial inactivation of 3-phosphatase activity
E195A/Y205A
Tequatrovirus T4
-
retains 22% activity of the wild type enzyme
E219A
Tequatrovirus T4
-
retains 51% activity of the wild type enzyme
E233A
Tequatrovirus T4
-
retains 45% activity of the wild type enzyme
E292A/W294A
Tequatrovirus T4
-
retains 3% activity of the wild type enzyme
G212A
Tequatrovirus T4
-
retains 37% activity of the wild type enzyme
K198A
Tequatrovirus T4
-
retains 82% activity of the wild type enzyme
K253A
Tequatrovirus T4
-
retains 95% activity of the wild type enzyme
K258A
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
K258Q
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
K258R
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
M199A/Y200A
Tequatrovirus T4
-
retains 19% activity of the wild type enzyme
N190A/M192A
Tequatrovirus T4
-
retains 18% activity of the wild type enzyme
R126A
Tequatrovirus T4
-
inactivation of 5-kinase activity
R126K
Tequatrovirus T4
-
inactivation of 5-kinase activity
R126Q
Tequatrovirus T4
-
inactivation of 5-kinase activity
R229A
Tequatrovirus T4
-
retains 94% activity of the wild type enzyme
R246A
Tequatrovirus T4
-
partial inactivation of 3-phosphatase activity
R246K
Tequatrovirus T4
-
no inactivation
R279A
Tequatrovirus T4
-
partial inactivation of 3-phosphatase activity
R287A/Q295A
Tequatrovirus T4
-
retains 2% activity of the wild type enzyme
R38A
Tequatrovirus T4
-
inactivation of 5-kinase activity
R38K
Tequatrovirus T4
-
inactivation of 5-kinase activity
R38Q
Tequatrovirus T4
-
inactivation of 5-kinase activity
S211T
Tequatrovirus T4
-
shows 130% activity of the wild type enzyme
S298A/D300A
Tequatrovirus T4
-
retains 27% activity of the wild type enzyme
T222A
Tequatrovirus T4
-
retains 94% activity of the wild type enzyme
T251A
Tequatrovirus T4
-
shows 120% activity of the wild type enzyme
D560A
-
mutation abolishes phosphatase activity of the C-terminal domain Rnl1-(394-694)
K407A
-
mutation has no effect on phosphatase activity of the C-terminal domain Rnl1-(394-694)
D236A
-
64% as active as wild-type Pnkp in cleaving 2',3'-cAMP
D236A
-
decreased activity compared to the wild type enzyme
D236E
-
decreased activity compared to the wild type enzyme
D236E
-
decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
D236N
-
decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
D236N
-
similar activity compared to the wild type enzyme
D392E
-
decreased activity compared to the wild type enzyme
D392E
-
increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
D392N
-
decreased activity compared to the wild type enzyme
D392N
-
increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
H189A
-
17% as active as wild type Pnkp
H189A
-
decreased activity compared to the wild type enzyme
H189A
-
decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
H189D
-
decreased activity compared to the wild type enzyme
H189D
-
the mutation imposes strict specificity for a 2',3' cyclic phosphate, which is cleaved to form a single 2'-NMP product and shows increased activity compared to the wild type enzyme
H189E
-
decreased activity compared to the wild type enzyme
H189E
-
increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
H264A
-
10% as active as wild-type Pnkp in cleaving 2',3'-cAMP
H264A
-
decreased activity compared to the wild type enzyme
H376D
-
decreased activity compared to the wild type enzyme
H376D
-
decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
H376N
-
decreased activity compared to the wild type enzyme
H376N
-
decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
R237A
-
24% as active as wild-type Pnkp in cleaving 2',3'-cAMP
R237A
-
decreased activity compared to the wild type enzyme
R237K
-
increased activity compared to the wild type enzyme
R237K
-
increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
R237Q
-
decreased activity compared to the wild type enzyme
R237Q
-
increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP
D167N
Tequatrovirus T4
-
inactivation of 3-phosphatase activity
D167N
Tequatrovirus T4
-
the mutant converts a RNA 2',3'-cyclic phosphate end to RNA 3'-phosphate
S211A
Tequatrovirus T4
-
less than 1% activity of the wild type enzyme
S211A
Tequatrovirus T4
-
the mutant transiently accumulates phosphor-RNA during 2',3'-cyclic phosphate removal
additional information
-
kinase negative PNKP is generated by site-directed mutagenesis using RNAi-resistant PNKP cDNA. Phosphatase negative PNKP is generated by site-directed mutagenesis using RNAi-resistant PNKP cDNA, enzyme-deficient A-549 cells are constructed by expression of shRNA
additional information
-
expression of enzyme in bacteria lacking abasic endonuclease/3-phosphatase function confers resistance to methylmethane sulfonate
additional information
-
enzyme deletion mutant, does not affect cell growth but results in significant hypersensitivity to gamma-radiation or to camptothecin, expression of human enzyme in the mutant restores hypersensitivity
additional information
-
generation of pnk1pku70 and pnk1rhp51 double mutants, and pnk1 single mutants. Mutation pnk1apn2 is synthetically lethal. But the nth1pnk1apn2 and tdp1pnk1apn2 triple mutants are viable
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Habraken, Y.; Verly, W.G.
Further purification and characterization of the DNA 3-phosphatase from rat-liver chromatin which is also a polynucleotide 5-hydroxyl kinase
Eur. J. Biochem.
171
59-66
1988
Rattus norvegicus
brenda
Habraken, Y.; Verly, W.G.
Chromatin 3-phosphatase/5-OH kinase cannot transfer phosphate from 3 to 5 across a strand nick in DNA
Nucleic Acids Res.
14
8103-8110
1986
Rattus norvegicus
brenda
Habraken, Y.; Verly, W.G.
The DNA 3-phosphatase and 5-hydroxyl kinase of rat liver chromatin
FEBS Lett.
160
46-50
1983
Rattus norvegicus
brenda
Pheiffer, B.H.; Zimmerman, S.B.
3-Phosphatase activity of the DNA kinase from rat liver
Biochem. Biophys. Res. Commun.
109
1297-1302
1982
Rattus norvegicus
brenda
Sirotkin, K.; Cooley, W.; Runnels, J.; Snyder, L.R.
A role in true-late gene expression for the T4 bacteriophage 5 polynucleotide kinase 3 phosphatase
J. Mol. Biol.
123
221-233
1978
Tequatrovirus T4
brenda
Jilani, A.; Ramotar, D.; Slack, C.; Ong, C.; Yang, X.M.; Scherer, S.W.; Lasko, D.D.
Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage
J. Biol. Chem.
274
24176-24186
1999
Homo sapiens (Q96T60), Homo sapiens
brenda
Jilani, A.; Slack, C.; Matheos, D.; Zannis-Hadjopoulos, M.; Lasko, D.D.
Purification of a polynucleotide kinase from calf thymus, comparison of its 3-phosphatase domain with T4 polynucleotide kinase, and investigation of its effect on DNA replication in vitro
J. Cell. Biochem.
73
188-203
1999
Bos taurus
brenda
Wang, L.K.; Shuman, S.
Mutational analysis defines the 5'-kinase and 3'-phosphatase active sites of T4 polynucleotide kinase
Nucleic Acids Res.
30
1073-1080
2002
Tequatrovirus T4
brenda
Jilani, A.; Ramotar, D.
Purification and partial characterization of a DNA 3'-phosphatase from Schizosaccharomyces pombe
Biochemistry
41
7688-7694
2002
Schizosaccharomyces pombe (O13911), Schizosaccharomyces pombe
brenda
Deshpande, R.A.; Wilson, T.E.
Identification of DNA 3'-phosphatase active site residues and their differential role in DNA binding, mg(2+) coordination, and catalysis
Biochemistry
43
8579-8589
2004
Saccharomyces cerevisiae
brenda
Vance, J.R.; Wilson, T.E.
Uncoupling of 3'-phosphatase and 5'-kinase functions in budding yeast. Characterization of Saccharomyces cerevisiae DNA 3'-phosphatase (TPP1)
J. Biol. Chem.
276
15073-15081
2001
Saccharomyces mikatae (Q9HET9), Saccharomyces mikatae
brenda
Petrucco, S.; Volpi, G.; Bolchi, A.; Rivetti, C.; Ottonello, S.
A nick-sensing DNA 3'-repair enzyme from Arabidopsis
J. Biol. Chem.
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brenda
Meijer, M.; Karimi-Busheri, F.; Huang, T.Y.; Weinfeld, M.; Young, D.
Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by g-radiation or camptothecin in Schizosaccharomyces pombe
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Karumbati, A.S.; Deshpande, R.A.; Jilani, A.; Vance, J.R.; Ramotar, D.; Wilson, T.E.
The role of yeast DNA 3'-phosphatase Tpp1 and rad1/Rad10 endonuclease in processing spontaneous and induced base lesions
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Zhu, H.; Yin, S.; Shuman, S.
Characterization of polynucleotide kinase/phosphatase enzymes from Mycobacteriophages omega and Cjw1 and vibriophage KVP40
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Omegavirus omega, Kostyavirus CJW1
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Martins, A.; Shuman, S.
Characterization of a baculovirus enzyme with RNA ligase, polynucleotide 5'-Kinase, and polynucleotide 3'-phosphatase activities
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unidentified baculovirus
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Blondal, T.; Hjorleifsdottir, S.; Aevarsson, A.; Fridjonsson, O.H.; Skirnisdottir, S.; Wheat, J.O.; Hermannsdottir, A.G.; Hreggvidsson, G.O.; Smith, A.V.; Kristjansson, J.K.
Characterization of a 5'-polynucleotide kinase/3'-phosphatase from bacteriophage RM378
J. Biol. Chem.
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Rhodothermus phage RM378
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Keppetipola, N.; Shuman, S.
Distinct enzymic functional groups are required for the phosphomonoesterase and phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase/phosphatase
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Acetivibrio thermocellus
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Zuber, S.; Ngom-Bru, C.; Barretto, C.; Bruttin, A.; Brussow, H.; Denou, E.
Genome analysis of phage JS98 defines a fourth major subgroup of T4-like phages in Escherichia coli
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Escherichia phage JS98 (A8R9L0)
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Zhu, H.; Shuman, S.
Substrate specificity and structure-function analysis of the 3-phosphoesterase component of the bacterial NHEJ protein, DNA ligase D
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Tequatrovirus T4, Saccharomyces cerevisiae
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Keppetipola, N.; Shuman, S.
Characterization of the 2,3 cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage lambda phosphatase
Nucleic Acids Res.
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Acetivibrio thermocellus
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Zhu, H.; Smith, P.; Wang, L.K.; Shuman, S.
Structure-function analysis of the 3' phosphatase component of T4 polynucleotide kinase/phosphatase
Virology
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Tequatrovirus T4
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Murphy, G.; Sansbury, L.S.; Bergen, A.W.; Wang, Z.; Schatzkin, A.; Lehman, T.; Kalidindi, A.; Modali, R.; Lanza, E.
Polynucleotide kinase 3' phosphatase variant, dietary variables and risk of adenoma recurrence in the Polyp Prevention Trial
Eur. J. Cancer Prev.
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Homo sapiens (Q96T60)
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Freschauf, G.K.; Karimi-Busheri, F.; Ulaczyk-Lesanko, A.; Mereniuk, T.R.; Ahrens, A.; Koshy, J.M.; Rasouli-Nia, A.; Pasarj, P.; Holmes, C.F.; Rininsland, F.; Hall, D.G.; Weinfeld, M.
Identification of a small molecule inhibitor of the human DNA repair enzyme polynucleotide kinase/phosphatase
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Homo sapiens, Mus musculus, Schizosaccharomyces pombe
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Freschauf, G.K.; Mani, R.S.; Mereniuk, T.R.; Fanta, M.; Virgen, C.A.; Dianov, G.L.; Grassot, J.M.; Hall, D.G.; Weinfeld, M.
Mechanism of action of an imido-piperidine inhibitor of human polynucleotide kinase/phosphatase
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Homo sapiens
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Shen, J.; Gilmore, E.C.; Marshall, C.A.; Haddadin, M.; Reynolds, J.J.; Eyaid, W.; Bodell, A.; Barry, B.; Gleason, D.; Allen, K.; Ganesh, V.S.; Chang, B.S.; Grix, A.; Hill, R.S.; Topcu, M.; Caldecott, K.W.; Barkovich, A.J.; Walsh, C.A.
Mutations in PNKP cause microcephaly, seizures and defects in DNA repair
Nat. Genet.
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Homo sapiens
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Ali, A.A.; Jukes, R.M.; Pearl, L.H.; Oliver, A.W.
Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK
Nucleic Acids Res.
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Homo sapiens (Q96T60)
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Song, C.; Zhang, C.; Zhao, M.
Development of a high-throughput screening platform for DNA 3'-phosphatases and their inhibitors based on a universal molecular beacon and quantitative real-time PCR
Chem. Asian J.
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Tequatrovirus T4
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Mani, R.S.; Yu, Y.; Fang, S.; Lu, M.; Fanta, M.; Zolner, A.E.; Tahbaz, N.; Ramsden, D.A.; Litchfield, D.W.; Lees-Miller, S.P.; Weinfeld, M.
Dual modes of interaction between XRCC4 and polynucleotide kinase/phosphatase: implications for nonhomologous end joining
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Plasmodium falciparum
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Weinfeld, M.; Mani, R.S.; Abdou, I.; Aceytuno, R.D.; Glover, J.N.
Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair
Trends Biochem. Sci.
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Homo sapiens, Mus musculus
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Kashkina, E.; Qi, T.; Weinfeld, M.; Young, D.
Polynucleotide kinase/phosphatase, Pnk1, is involved in base excision repair in Schizosaccharomyces pombe
DNA Repair
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2012
Schizosaccharomyces pombe
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Siribal, S.; Weinfeld, M.; Karimi-Busheri, F.; Mark Glover, J.N.; Bernstein, N.K.; Aceytuno, D.; Chavalitshewinkoon-Petmitr, P.
Molecular characterization of Plasmodium falciparum putative polynucleotide kinase/phosphatase
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Plasmodium falciparum
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Tahbaz, N.; Subedi, S.; Weinfeld, M.
Role of polynucleotide kinase/phosphatase in mitochondrial DNA repair
Nucleic Acids Res.
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Homo sapiens
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Liu, X.; Ge, J.; Wang, X.; Wu, Z.; Shen, G.; Yu, R.
Development of a highly sensitive sensing platform for T4 polynucleotide kinase phosphatase and its inhibitors based on WS2 nanosheets
Anal. Methods
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Tequatrovirus T4
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brenda
Jiang, H.X.; Kong, D.M.; Shen, H.X.
Amplified detection of DNA ligase and polynucleotide kinase/phosphatase on the basis of enrichment of catalytic G-quadruplex DNAzyme by rolling circle amplification
Biosens. Bioelectron.
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Tequatrovirus T4
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Della-Maria, J.; Hegde, M.L.; McNeill, D.R.; Matsumoto, Y.; Tsai, M.S.; Ellenberger, T.; Wilson, D.M.; Mitra, S.; Tomkinson, A.E.
The interaction between polynucleotide kinase phosphatase and the DNA repair protein XRCC1 is critical for repair of DNA alkylation damage and stable association at DNA damage sites
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Homo sapiens
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Shirodkar, P.; Fenton, A.L.; Meng, L.; Koch, C.A.
Identification and functional characterization of a Ku-binding motif in aprataxin polynucleotide kinase/phosphatase-like factor (APLF)
J. Biol. Chem.
288
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Homo sapiens
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Das, U.; Shuman, S.
Mechanism of RNA 2,3-cyclic phosphate end healing by T4 polynucleotide kinase-phosphatase
Nucleic Acids Res.
41
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Tequatrovirus T4
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Ma, C.; Jin, S.; Wang, J.; Wang, K.; Liu, H.; Wu, K.
A fluorescence-based assay for T4 polynucleotide kinase/phosphatase activity based on a terminal transferase-aided photoinduced electron transfer strategy
Anal. Methods
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1989-1994
2016
Tequatrovirus T4 (P06855)
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brenda
Havali-Shahriari, Z.; Weinfeld, M.; Glover, J.N.
Characterization of DNA substrate binding to the phosphatase domain of the DNA repair enzyme polynucleotide kinase/phosphatase
Biochemistry
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Mus musculus (Q9JLV6)
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Shimada, M.; Dumitrache, L.C.; Russell, H.R.; McKinnon, P.J.
Polynucleotide kinase-phosphatase enables neurogenesis via multiple DNA repair pathways to maintain genome stability
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Mus musculus (Q9JLV6), Mus musculus
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Zhang, X.; Liu, Q.; Jin, Y.; Li, B.
Determination of the activity of T4 polynucleotide kinase phosphatase by exploiting the sequence-dependent fluorescence of DNA-templated copper nanoclusters
Microchim. Acta
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Tequatrovirus T4 (P06855)
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Chatterjee, A.; Saha, S.; Chakraborty, A.; Silva-Fernandes, A.; Mandal, S.M.; Neves-Carvalho, A.; Liu, Y.; Pandita, R.K.; Hegde, M.L.; Hegde, P.M.; Boldogh, I.; Ashizawa, T.; Koeppen, A.H.; Pandita, T.K.; Maciel, P.; Sarkar, P.S.; Hazra, T.K.
The role of the mammalian DNA end-processing enzyme polynucleotide kinase 3-phosphatase in spinocerebellar ataxia type 3 pathogenesis
PLoS Genet.
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2015
Homo sapiens, Mus musculus (Q9JLV6), Mus musculus
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Dong, Z.; Zhang, L.; Qiao, M.; Ge, J.; Liu, A.; Li, Z.
A label-free assay for T4 polynucleotide kinase/phosphatase activity and its inhibitors based on poly(thymine)-templated copper nanoparticles
Talanta
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253-258
2015
Tequatrovirus T4 (P06855)
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