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Literature summary extracted from

  • Schellenberg, M.; Williams, R.
    DNA end processing by polynucleotide kinase/phosphatase (2011), Proc. Natl. Acad. Sci. USA, 108, 20855-20856.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.78 inactivated PNK mutant protein with several 3'-phosphorylated DNAs of different sequence bound in the phosphatase active site Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.78 additional information productive engagement of a 3'-phosphate terminus may block access of a 5'-hydroxyl to the kinase active site Homo sapiens
2.7.1.78 additional information productive engagement of a 3'-phosphate terminus may block access of a 5'-hydroxyl to the kinase active site Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.78 Mg2+ required Mus musculus
2.7.1.78 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.78 ATP + 5'-dephospho-DNA Mus musculus
-
 ADP + 5'-phospho-DNA
-
 ?
2.7.1.78 ATP + 5'-dephospho-DNA Homo sapiens
-
 ADP + 5'-phospho-DNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.78 Homo sapiens
-
-
-
2.7.1.78 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.78 ATP + 5'-dephospho-DNA
-
 Mus musculus ADP + 5'-phospho-DNA
-
 ?
2.7.1.78 ATP + 5'-dephospho-DNA
-
 Homo sapiens ADP + 5'-phospho-DNA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.78 More separate kinase and phosphatase catalytic activities are located in two halves of an interconnected bilobed catalytic domain that is flexibly linked to an aminoterminal phosphoprotein-binding forkhead-associated domain Mus musculus
2.7.1.78 More separate kinase and phosphatase catalytic activities are located in two halves of an interconnected bilobed catalytic domain that is flexibly linked to an aminoterminal phosphoprotein-binding forkhead-associated domain Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.7.1.78 PNK
-
 Mus musculus
2.7.1.78 PNK
-
 Homo sapiens
2.7.1.78 PNKP
-
 Mus musculus
2.7.1.78 PNKP
-
 Homo sapiens
2.7.1.78 polynucleotide kinase/phosphatase
-
 Mus musculus
2.7.1.78 polynucleotide kinase/phosphatase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.78 ATP
-
 Mus musculus
2.7.1.78 ATP
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.1.78 additional information PNK domain architecture, overview Mus musculus
2.7.1.78 additional information PNK domain architecture, overview Homo sapiens
2.7.1.78 physiological function bifunctional polynucleotide kinase/phosphatase contains both DNA 5'-kinase and 3'-phosphatase activities required for restoration of 3'-hydroxyls and 5'-phosphates needed to seal the broken DNA. Cellular DNA is constantly assaulted by ionizing radiation and reactive oxygen species. This damage, along with the products of some DNA repair enzymes, may contain 5' hydroxyls or 3' phosphates. These are converted by PNK to 5' phosphates and 3' hydroxyls, which are required for DNA polymerases and DNA ligases to complete repair of the damaged DNA. Productive engagement of a 3'-phosphate terminus may block access of a 5'-hydroxyl to the kinase active site Mus musculus
2.7.1.78 physiological function bifunctional polynucleotide kinase/phosphatase contains both DNA 5'-kinase and 3'-phosphatase activities required for restoration of 3'-hydroxyls and 5'-phosphates needed to seal the broken DNA. Cellular DNA is constantly assaulted by ionizing radiation and reactive oxygen species. This damage, along with the products of some DNA repair enzymes, may contain 5' hydroxyls or 3' phosphates. These are converted by PNK to 5' phosphates and 3' hydroxyls, which are required for DNA polymerases and DNA ligases to complete repair of the damaged DNA. Productive engagement of a 3'-phosphate terminus may block access of a 5'-hydroxyl to the kinase active site Homo sapiens