関: DNA kinase、polynucleotide 5'-hydroxyl-kinase

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an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
the basic unit of money in Papua New Guinea

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/03/23 16:23:21」(JST)

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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 a ligation reaction.

Nomenclature[edit]

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as 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. 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[edit]

Vivo
New England Biolabs' T4 PNK page

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English Journal

Label free fluorescence turn-on detection of polynucleotide kinase activity with a perylene probe.

Jiao H, Wang B, Chen J, Liao D, Li W, Yu C.SourceState Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, P. R. China. congyu@ciac.jl.cn.
Chemical communications (Cambridge, England).Chem Commun (Camb).2012 Aug 14;48(63):7862-4. Epub 2012 Jul 2.
A single stranded oligonucleotide could induce aggregation of a perylene probe, the probe's monomer fluorescence was efficiently quenched. However, when the oligonucleotide was 5'-phosphorylated by polynucleotide kinase, it could be very efficiently degraded by lambda exonuclease, probe monomers wer
PMID 22786467

Molecular basis of bacterial protein Hen1 activating the ligase activity of bacterial protein Pnkp for RNA repair.

Wang P, Chan CM, Christensen D, Zhang C, Selvadurai K, Huang RH.SourceDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2012 Aug 14;109(33):13248-53. Epub 2012 Jul 30.
Ribotoxins cleave essential RNAs for cell killing in vivo, and the bacterial polynucleotide kinase-phosphatase (Pnkp)/hua enhancer 1 (Hen1) complex has been shown to repair ribotoxin-cleaved RNAs in vitro. Bacterial Pnkp/Hen1 is distinguished from other RNA repair systems by performing 3'-terminal 2
PMID 22847431

Japanese Journal

Comparison of the molecular influences of NO-induced lesions in DNA strands on the reactivity of polynucleotide kinases, DNA ligases and DNA polymerases

Doi Akihiro,Pack Seung Pil,Makino Keisuke
The journal of biochemistry 147(5), 697-703, 2010-05-01
NAID 10027875826

.BETA.-Sitosteryl (6'-O-linoleoyl)-glucoside of Soybean (Glycine max L.) Crude Extract Inhibits Y-Family DNA Polymerases

, , [他], , , , , , ,
Journal of Oleo Science 59(11), 621-630, 2010
… In addition, compound 1 had no effect on prokaryotic pols or other DNA metabolic enzymes such as calf primase of pol α, T7 RNA polymerase, T4 polynucleotide kinase, or bovine deoxyribonuclease I. …
NAID 130000437428

Involvement of polynucleotide kinase in a poly(ADP-ribose) polymerase-1-dependent DNA double-strand breaks rejoining pathway

AUDEBERT M
J Mol Biol 356, 257-265, 2006
NAID 30018474924

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リンク元	「ポリヌクレオチドキナーゼ」「polynucleotide 5'-hydroxyl-kinase」「DNA kinase」
関連記事	「kinase」

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ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase
Identifiers
EC number	2.7.1.78
CAS number	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 / EGO
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NCBI	proteins