Enzymes
| UniProtKB help_outline | 536 proteins |
Reaction participants Show >> << Hide
- Name help_outline 2-oxoglutarate Identifier CHEBI:16810 (Beilstein: 3664503; CAS: 64-15-3) help_outline Charge -2 Formula C5H4O5 InChIKeyhelp_outline KPGXRSRHYNQIFN-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 418 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-histidyl-[ribosomal protein uL15]
Identifier
RHEA-COMP:13760
Reactive part
help_outline
- Name help_outline L-histidine residue Identifier CHEBI:29979 Charge 0 Formula C6H7N3O SMILEShelp_outline C(*)(=O)[C@@H](N*)CC=1N=CNC1 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
(3S)-3-hydroxy-L-histidyl-[ribosomal protein uL15]
Identifier
RHEA-COMP:13761
Reactive part
help_outline
- Name help_outline (3S)-3-hydroxy-L-histidine residue Identifier CHEBI:138021 Charge 0 Formula C6H7N3O2 SMILEShelp_outline C(*)(=O)[C@@H](N*)[C@@H](C=1N=CNC1)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 CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 980 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline succinate Identifier CHEBI:30031 (Beilstein: 1863859; CAS: 56-14-4) help_outline Charge -2 Formula C4H4O4 InChIKeyhelp_outline KDYFGRWQOYBRFD-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 325 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:54024 | RHEA:54025 | RHEA:54026 | RHEA:54027 | |
|---|---|---|---|---|
| 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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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans.
Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N., Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D., Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C., Jiang M., Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A., Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M., Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L., Schofield C.J.
The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylati ... >> More
The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes. << Less
Nat. Chem. Biol. 8:960-962(2012) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.