Enzymes
| UniProtKB help_outline | 719 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
a 5'-end FAD-phospho-ribonucleoside in mRNA
Identifier
RHEA-COMP:17275
Reactive part
help_outline
- Name help_outline 5'-FAD-phospho-ribonucleoside residue Identifier CHEBI:172372 Charge -4 Formula C32H36N9O21P3R SMILEShelp_outline N1(C2=C(C(=NC=N2)N)N=C1)[C@@H]3O[C@H](COP(OP(OC[C@H]([C@@H](O)[C@H](CN4C=5C(=NC6=C4C=C(C)C(=C6)C)C([N-]C(N5)=O)=O)O)O)(=O)[O-])(=O)[O-])[C@H]([C@H]3O)OP(OC[C@H]7O[C@H]([C@@H]([C@@H]7O*)O)*)(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 2 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-adenosine-phospho-ribonucleoside in mRNA
Identifier
RHEA-COMP:15719
Reactive part
help_outline
- Name help_outline 5'-end phospho-adenosine-phospho-ribonucleoside residue Identifier CHEBI:144051 Charge -3 Formula C15H18N5O13P2R SMILEShelp_outline [C@@H]1(O[C@H]([C@@H]([C@@H]1OP(OC[C@H]2O[C@H]([C@@H]([C@@H]2O*)O)*)(=O)[O-])O)N3C4=C(C(=NC=N4)N)N=C3)COP([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 FMN Identifier CHEBI:58210 Charge -3 Formula C17H18N4O9P InChIKeyhelp_outline ANKZYBDXHMZBDK-SCRDCRAPSA-K SMILEShelp_outline C12=NC([N-]C(C1=NC=3C(N2C[C@@H]([C@@H]([C@@H](COP(=O)([O-])[O-])O)O)O)=CC(=C(C3)C)C)=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 781 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
Cross-references
| RHEA:67588 | RHEA:67589 | RHEA:67590 | RHEA:67591 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs.
Sharma S., Grudzien-Nogalska E., Hamilton K., Jiao X., Yang J., Tong L., Kiledjian M.
We recently reported the presence of nicotinamide adenine dinucleotide (NAD)-capped RNAs in mammalian cells and a role for DXO and the Nudix hydrolase Nudt12 in decapping NAD-capped RNAs (deNADding) in cells. Analysis of 5'caps has revealed that in addition to NAD, mammalian RNAs also contain othe ... >> More
We recently reported the presence of nicotinamide adenine dinucleotide (NAD)-capped RNAs in mammalian cells and a role for DXO and the Nudix hydrolase Nudt12 in decapping NAD-capped RNAs (deNADding) in cells. Analysis of 5'caps has revealed that in addition to NAD, mammalian RNAs also contain other metabolite caps including flavin adenine dinucleotide (FAD) and dephosphoCoA (dpCoA). In the present study we systematically screened all mammalian Nudix proteins for their potential deNADing, FAD cap decapping (deFADding) and dpCoA cap decapping (deCoAping) activity. We demonstrate that Nudt16 is a novel deNADding enzyme in mammalian cells. Additionally, we identified seven Nudix proteins-Nudt2, Nudt7, Nudt8, Nudt12, Nudt15, Nudt16 and Nudt19, to possess deCoAping activity in vitro. Moreover, our screening revealed that both mammalian Nudt2 and Nudt16 hydrolyze FAD-capped RNAs in vitro with Nudt16 regulating levels of FAD-capped RNAs in cells. All decapping activities identified hydrolyze the metabolite cap substrate within the diphosphate linkage. Crystal structure of human Nudt16 in complex with FAD at 2.7 Å resolution provide molecular insights into the binding and metal-coordinated hydrolysis of FAD by Nudt16. In summary, our study identifies novel cellular deNADding and deFADding enzymes and establishes a foundation for the selective functionality of the Nudix decapping enzymes on non-canonical metabolite caps. << Less
Nucleic Acids Res. 48:6788-6798(2020) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.