ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.1.78 | ||||||||
CAS no. | 37211-65-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a polynucleotide 5'-hydroxyl-kinase (EC 2.7.1.78) is an enzyme that catalyzes the chemical reaction
- 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
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
- 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. 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. PMID 4287930.
External links