Polynucleotide 5'-hydroxyl-kinase

In enzymology, a polynucleotide 5'-hydroxyl-kinase (EC 2.7.1.78) is an enzyme that catalyzes the chemical reaction

ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase
Identifiers
EC no.2.7.1.78
CAS no.37211-65-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
ATP + 5'-dephospho-DNA ADP + 5'-phospho-DNA

Thus, the two substrates of this enzyme are ATP and 5'-dephospho-DNA, whereas its two products are ADP and 5'-phospho-DNA. Polynucleotide kinase is a T7 bacteriophage (or T4 bacteriophage) enzyme that catalyzes the transfer of a gamma-phosphate from ATP to the free hydroxyl end of the 5' DNA or RNA. The resulting product could be used to end-label DNA or RNA, or in ligation reactions.

Nomenclature

edit

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as an acceptor. The systematic name of this enzyme class is ATP:5'-dephosphopolynucleotide 5'-phosphotransferase. Other names in common use include:

  • ATP:5'-dephosphopolynucleotide 5'-phosphatase
  • PNK
  • polynucleotide 5'-hydroxyl kinase (phosphorylating),
  • 5'-hydroxyl polynucleotide kinase,
  • 5'-hydroxyl polyribonucleotide kinase,
  • 5'-hydroxyl RNA kinase,
  • DNA 5'-hydroxyl kinase,
  • DNA kinase,
  • polynucleotide kinase, and
  • polynucleotide 5'-hydroxy-kinase.

References

edit
  • Novogrodsky A, Hurwitz J (1966). "The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. I. Phosphorylation at 5'-hydroxyl termini". J. Biol. Chem. 241 (12): 2923–32. doi:10.1016/S0021-9258(18)96553-1. PMID 4287929.
  • Novogrodsky A, Tal M, Traub A, Hurwitz J (1966). "The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. II. Further properties of the 5'-hydroxyl polynucleotide kinase". J. Biol. Chem. 241 (12): 2933–43. doi:10.1016/S0021-9258(18)96554-3. PMID 4287930.
edit