Enzymes
UniProtKB help_outline | 1,731 proteins |
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Namehelp_outline
a 5'-end NAD+-phospho-ribonucleoside in mRNA
Identifier
RHEA-COMP:15698
Reactive part
help_outline
- Name help_outline a 5'-end NAD+-phospho-ribonucleoside residue Identifier CHEBI:144029 Charge -2 Formula C26H32N7O20P3R SMILEShelp_outline N1(C2=C(C(=NC=N2)N)N=C1)[C@@H]3O[C@H](COP(OP(OC[C@H]4O[C@@H]([N+]5=CC(=CC=C5)C(=O)N)[C@@H]([C@@H]4O)O)(=O)[O-])(=O)[O-])[C@H]([C@H]3O)OP(OC[C@H]6O[C@H]([C@@H]([C@@H]6O*)O)*)(=O)[O-] 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 H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 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 phospho-ribonucleoside in mRNA
Identifier
RHEA-COMP:15692
Reactive part
help_outline
- Name help_outline 5'-end ribonucleotide residue Identifier CHEBI:138282 Charge -2 Formula C5H7O7PR SMILEShelp_outline [C@@H]1(O[C@H]([C@@H]([C@@H]1O*)O)*)COP([O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 27 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:60880 | RHEA:60881 | RHEA:60882 | RHEA:60883 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Gene Ontology help_outline |
Publications
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Eukaryotic RNA 5'-End NAD<sup>+</sup> Capping and DeNADding.
Kiledjian M.
A hallmark of eukaryotic mRNAs has long been the 5'-end m<sup>7</sup>G cap. This paradigm was recently amended by recent reports that Saccharomyces cerevisiae and mammalian cells also contain mRNAs carrying a novel nicotinamide adenine dinucleotide (NAD<sup>+</sup>) cap at their 5'-end. The presen ... >> More
A hallmark of eukaryotic mRNAs has long been the 5'-end m<sup>7</sup>G cap. This paradigm was recently amended by recent reports that Saccharomyces cerevisiae and mammalian cells also contain mRNAs carrying a novel nicotinamide adenine dinucleotide (NAD<sup>+</sup>) cap at their 5'-end. The presence of an NAD<sup>+</sup> cap on mRNA uncovers a previously unknown mechanism for controlling gene expression through nucleotide metabolite-directed mRNA turnover. In contrast to the m<sup>7</sup>G cap that stabilizes mRNA, the NAD<sup>+</sup> cap targets RNA for rapid decay in mammalian cells through the DXO non-canonical decapping enzyme which removes intact NAD<sup>+</sup> from RNA in a process termed 'deNADding'. This review highlights the identification of NAD<sup>+</sup> caps, their mode of addition, and their functional significance in cells. << Less
Trends Cell Biol 28:454-464(2018) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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5' end nicotinamide adenine dinucleotide cap in human cells promotes RNA decay through DXO-mediated deNADding.
Jiao X., Doamekpor S.K., Bird J.G., Nickels B.E., Tong L., Hart R.P., Kiledjian M.
Eukaryotic mRNAs generally possess a 5' end N7 methyl guanosine (m<sup>7</sup>G) cap that promotes their translation and stability. However, mammalian mRNAs can also carry a 5' end nicotinamide adenine dinucleotide (NAD<sup>+</sup>) cap that, in contrast to the m<sup>7</sup>G cap, does not support ... >> More
Eukaryotic mRNAs generally possess a 5' end N7 methyl guanosine (m<sup>7</sup>G) cap that promotes their translation and stability. However, mammalian mRNAs can also carry a 5' end nicotinamide adenine dinucleotide (NAD<sup>+</sup>) cap that, in contrast to the m<sup>7</sup>G cap, does not support translation but instead promotes mRNA decay. The mammalian and fungal noncanonical DXO/Rai1 decapping enzymes efficiently remove NAD<sup>+</sup> caps, and cocrystal structures of DXO/Rai1 with 3'-NADP<sup>+</sup> illuminate the molecular mechanism for how the "deNADding" reaction produces NAD<sup>+</sup> and 5' phosphate RNA. Removal of DXO from cells increases NAD<sup>+</sup>-capped mRNA levels and enables detection of NAD<sup>+</sup>-capped intronic small nucleolar RNAs (snoRNAs), suggesting NAD<sup>+</sup> caps can be added to 5'-processed termini. Our findings establish NAD<sup>+</sup> as an alternative mammalian RNA cap and DXO as a deNADding enzyme modulating cellular levels of NAD<sup>+</sup>-capped RNAs. Collectively, these data reveal that mammalian RNAs can harbor a 5' end modification distinct from the classical m<sup>7</sup>G cap that promotes rather than inhibits RNA decay. << Less
Cell 168:1015-1027(2017) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs.
Doamekpor S.K., Grudzien-Nogalska E., Mlynarska-Cieslak A., Kowalska J., Kiledjian M., Tong L.
In eukaryotes, the DXO/Rai1 enzymes can eliminate most of the incomplete and non-canonical NAD caps through their decapping, deNADding and pyrophosphohydrolase activities. Here, we report that these enzymes can also remove FAD and dephospho-CoA (dpCoA) non-canonical caps from RNA, and we have name ... >> More
In eukaryotes, the DXO/Rai1 enzymes can eliminate most of the incomplete and non-canonical NAD caps through their decapping, deNADding and pyrophosphohydrolase activities. Here, we report that these enzymes can also remove FAD and dephospho-CoA (dpCoA) non-canonical caps from RNA, and we have named these activities deFADding and deCoAping. The crystal structures of mammalian DXO with 3'-FADP or CoA and fission yeast Rai1 with 3'-FADP provide elegant insight to these activities. FAD and CoA are accommodated in the DXO/Rai1 active site by adopting folded conformations. The flavin of FAD and the pantetheine group of CoA contact the same region at the bottom of the active site tunnel, which undergoes conformational changes to accommodate the different cap moieties. We have developed FAD-capQ to detect and quantify FAD-capped RNAs and determined that FAD caps are present on short RNAs (with less than ∼200 nucleotides) in human cells and that these RNAs are stabilized in the absence of DXO. << Less
Nucleic Acids Res. 48:6136-6148(2020) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.