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Literature summary for 2.7.1.78 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
Search for more literature for 2.7.1.78

Crystallization (Commentary)

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

Inhibitors

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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mus musculus
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
additional information PNK domain architecture, overview Mus musculus
additional information PNK domain architecture, overview Homo sapiens
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
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