Reaction participants Show >> << Hide
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Namehelp_outline
a 5'-end dephospho-2'-deoxyribonucleoside-DNA
Identifier
RHEA-COMP:13184
Reactive part
help_outline
- Name help_outline 5'-end 2'-deoxyribonucleoside Identifier CHEBI:136416 Charge 0 Formula C5H8O3R SMILEShelp_outline OC[C@H]1O[C@@H](*)C[C@@H]1O* 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,284 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA
Identifier
RHEA-COMP:13180
Reactive part
help_outline
- Name help_outline 5'-phosphate 2'-deoxynucleoside residue Identifier CHEBI:136412 Charge -2 Formula C5H7O6PR SMILEShelp_outline *[C@@H]1O[C@H](COP(=O)([O-])[O-])[C@@H](O*)C1 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 841 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:15669 | RHEA:15670 | RHEA:15671 | RHEA:15672 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. I. Phosphorylation at 5'-hydroxyl termini.
Novogrodsky A., Hurwitz J.
J Biol Chem 241:2923-2932(1966) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Characterization of a thermostable archaeal polynucleotide kinase homologous to human Clp1.
Jain R., Shuman S.
Clp1 proteins are essential components of the eukaryal mRNA 3' cleavage-polyadenylation machinery. Human Clp1 has an additional function as an RNA-specific 5'-OH polynucleotide kinase, which is implicated in RNA end healing. Yeast Clp1 has no kinase activity, although it binds ATP. Here we report ... >> More
Clp1 proteins are essential components of the eukaryal mRNA 3' cleavage-polyadenylation machinery. Human Clp1 has an additional function as an RNA-specific 5'-OH polynucleotide kinase, which is implicated in RNA end healing. Yeast Clp1 has no kinase activity, although it binds ATP. Here we report that Clp1-like proteins are extant in archaea. Purification and characterization of Pyrococcus horikoshii Clp1 (PhoClp1) reveals it to be a thermostable 5'-OH polynucleotide kinase optimally active at 55 degrees C to 85 degrees C. PhoClp1 catalyzes transfer of the gamma phosphate from ATP (K (m) 16 microM) to either 5'-OH RNA or DNA ends, although it prefers RNA in a competitive situation. Increasing the monovalent salt concentration to 250 mM suppresses the DNA kinase without affecting RNA phosphorylation, suggesting that RNA is a likely substrate for this enzyme in vivo. Indeed, we show that expression of PhoClp1 in budding yeast can complement a lethal mutation in the 5'-OH RNA kinase module of tRNA ligase. PhoClp1 is a member of the P-loop phosphotransferase superfamily. Alanine mutations at the P-loop lysine (Lys49) and a conserved aspartate (Asp73) inactivate the kinase. Our studies fortify emerging evidence for an enzymatic RNA repair capacity in archaea and provide a new reagent for polynucleotide phosphorylation at high temperatures. << Less
RNA 15:923-931(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. II. Further properties of the 5'-hydroxyl polynucleotide kinase.
Novogrodsky A., Tal M., Traub A., Hurwitz J.
J Biol Chem 241:2933-2943(1966) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.