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Literature summary for 3.1.3.32 extracted from

  • 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 (2011), Trends Biochem. Sci., 36, 262-271.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.32

Activating Compound

Activating Compound Comment Organism Structure
XRCC1 DNA repair scaffold protein, mechanism, overview Mus musculus
XRCC1 DNA repair scaffold protein, mechanism, overview Homo sapiens
XRCC4 DNA repair scaffold protein, mechanism, overview Mus musculus
XRCC4 DNA repair scaffold protein, mechanism, overview Homo sapiens

Application

Application Comment Organism
pharmacology PNKP, similar to several other DNA repair proteins, is of increasing clinical interest owing to the identification of small molecule inhibitors of these enzymes that sensitize cells to IR or chemotherapeutic agents Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens structure of the human PNKP FHA domain bound to a doubly phosphorylated phosphopeptide derived from XRCC1, overview ?
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
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 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information structure of the human PNKP FHA domain bound to a doubly phosphorylated phosphopeptide derived from XRCC1, overview Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More PNK phosphatase is a multidomain enzyme that consists of an N-terminal forkhead-associated domain and a C-terminal catalytic domain composed of fused phosphatase and kinase subdomains, structure of mammalian PNK phosphatase, overview Mus musculus
More PNK phosphatase is a multidomain enzyme that consists of an N-terminal forkhead-associated domain and a C-terminal catalytic domain composed of fused phosphatase and kinase subdomains, structure of mammalian PNK phosphatase, overview Homo sapiens

Synonyms

Synonyms Comment Organism
PNKP
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 Mus musculus
PNKP
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 Homo sapiens
polynucleotide kinase/phosphatase
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 Mus musculus
polynucleotide kinase/phosphatase
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 Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens
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 Homo sapiens
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 Mus musculus
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 Mus musculus
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 Homo sapiens