3.1.3.32: polynucleotide 3'-phosphatase
This is an abbreviated version!
For detailed information about polynucleotide 3'-phosphatase, go to the full flat file.
Word Map on EC 3.1.3.32
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3.1.3.32
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3'-phosphate
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exonuclease
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5'-kinase
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ape1
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5\'-hydroxyl
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3'-blocking
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xrcc4
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end-healing
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apraxia
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apurinic
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aprataxin
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diesterase
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end-processing
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3'-phosphorylated
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strand-breaks
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3'-phosphoesterase
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3'-phosphoglycolate
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phosphoesterase
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tyrosyl-dna
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analysis
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ap-endonuclease
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pharmacology
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medicine
- 3.1.3.32
- 3'-phosphate
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exonuclease
-
5'-kinase
- ape1
-
5\'-hydroxyl
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3'-blocking
- xrcc4
-
end-healing
- apraxia
-
apurinic
- aprataxin
- diesterase
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end-processing
-
3'-phosphorylated
-
strand-breaks
-
3'-phosphoesterase
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3'-phosphoglycolate
-
phosphoesterase
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tyrosyl-dna
- analysis
- ap-endonuclease
- pharmacology
- medicine
Reaction
Synonyms
2'(3')-polynucleotidase, 3' phosphatase, 3'-phosphatase, 3'-phosphatase/5'-OH kinase, 5' polynucleotidekinase 3' phosphatase, 5'-polynucleotide kinase/3'-phosphatase, APLF, APTX/PNKP-like factor, AtZDP, chromatin 3'-phosphatase, deoxyribonucleate 3'-phosphatase, DNA 3'-phosphatase, phosphatase, polynucleotide 3'-, Pnk1, PNKP, polynucleotide kinase 3'-phosphatase, polynucleotide kinase phosphatase, polynucleotide kinase-phosphatase, polynucleotide kinase/phosphatase, RNA ligase 1, Rnl1, SNQI-PNK, T4 polynucleotide kinase/phosphatase, Tpp1
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General Information
General Information on EC 3.1.3.32 - polynucleotide 3'-phosphatase
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evolution
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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
metabolism
physiological function
additional information
malfunction
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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
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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
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Pnk1 and Apn2 may function in parallel pathways essential for the repair of endogenous DNA damage
metabolism
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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
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interaction between XRCC1 and polynucleotide kinase 3'-phosphatase is critical for the retention of XRCC1 at DNA damage sites and DNA damage repair
Tequatrovirus T4
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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
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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
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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
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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
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the enzyme is involved in repair of DNA single and double strand breaks following exposure of cells to ionizing radiation
physiological function
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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
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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
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the mitochondrial enzyme polynucleotide kinase/phosphatase is required in mitochondrial DNA repair, overview
physiological function
Tequatrovirus T4
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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
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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
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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
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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