Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
N1-methylpseudouridine1191 in yeast 18S rRNA
Identifier
RHEA-COMP:13852
Reactive part
help_outline
- Name help_outline N1-methylpseudouridine 5'-phosphate residue Identifier CHEBI:74890 Charge -1 Formula C10H12N2O8P Positionhelp_outline 1191 SMILEShelp_outline C=1N(C(NC(C1[C@@H]2O[C@H](COP(*)(=O)[O-])[C@H]([C@H]2O)O*)=O)=O)C 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 S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 868 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N1-methyl-N3-[(3S)-3-amino-3-carboxypropyl]pseudouridine1191 in yeast 18S rRNA
Identifier
RHEA-COMP:16309
Reactive part
help_outline
- Name help_outline N1-methyl-N3-[(3S)-3-amino-3-carboxypropyl]-pseudouridine residue Identifier CHEBI:146234 Charge -1 Formula C14H19N3O10P Positionhelp_outline 1191 SMILEShelp_outline C=1N(C(N(C(C1[C@@H]2O[C@H](COP(*)(=O)[O-])[C@H]([C@H]2O)O*)=O)CC[C@@H](C([O-])=O)[NH3+])=O)C 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 S-methyl-5'-thioadenosine Identifier CHEBI:17509 (Beilstein: 42420; CAS: 2457-80-9) help_outline Charge 0 Formula C11H15N5O3S InChIKeyhelp_outline WUUGFSXJNOTRMR-IOSLPCCCSA-N SMILEShelp_outline CSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 34 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:63300 | RHEA:63301 | RHEA:63302 | RHEA:63303 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Ribosome biogenesis factor Tsr3 is the aminocarboxypropyl transferase responsible for 18S rRNA hypermodification in yeast and humans.
Meyer B., Wurm J.P., Sharma S., Immer C., Pogoryelov D., Koetter P., Lafontaine D.L., Woehnert J., Entian K.D.
The chemically most complex modification in eukaryotic rRNA is the conserved hypermodified nucleotide N1-methyl-N3-aminocarboxypropyl-pseudouridine (m(1)acp(3)Ψ) located next to the P-site tRNA on the small subunit 18S rRNA. While S-adenosylmethionine was identified as the source of the aminocarbo ... >> More
The chemically most complex modification in eukaryotic rRNA is the conserved hypermodified nucleotide N1-methyl-N3-aminocarboxypropyl-pseudouridine (m(1)acp(3)Ψ) located next to the P-site tRNA on the small subunit 18S rRNA. While S-adenosylmethionine was identified as the source of the aminocarboxypropyl (acp) group more than 40 years ago the enzyme catalyzing the acp transfer remained elusive. Here we identify the cytoplasmic ribosome biogenesis protein Tsr3 as the responsible enzyme in yeast and human cells. In functionally impaired Tsr3-mutants, a reduced level of acp modification directly correlates with increased 20S pre-rRNA accumulation. The crystal structure of archaeal Tsr3 homologs revealed the same fold as in SPOUT-class RNA-methyltransferases but a distinct SAM binding mode. This unique SAM binding mode explains why Tsr3 transfers the acp and not the methyl group of SAM to its substrate. Structurally, Tsr3 therefore represents a novel class of acp transferase enzymes. << Less
Nucleic Acids Res. 44:4304-4316(2016) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.