Enzymes
UniProtKB help_outline | 3,152 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
5-methylaminomethyl-S-(2E)-geranyl-thiouridine34 in tRNA
Identifier
RHEA-COMP:14654
Reactive part
help_outline
- Name help_outline 5-methylaminomethyl-S-(2E)-geranyl-thiouridine 5'-monophosphate residue Identifier CHEBI:140632 Charge 0 Formula C21H32N3O7PS SMILEShelp_outline [C@@H]1(N2C(=NC(=O)C(=C2)C[NH2+]C)SC/C=C(/CCC=C(C)C)\C)O[C@H](COP(*)(=O)[O-])[C@H]([C@H]1O)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 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
- Name help_outline selenophosphate Identifier CHEBI:16144 Charge -3 Formula O3PSe InChIKeyhelp_outline JRPHGDYSKGJTKZ-UHFFFAOYSA-K SMILEShelp_outline [O-]P([O-])([O-])=[Se] 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2E)-thiogeraniol Identifier CHEBI:143703 (CAS: 39067-80-6) help_outline Charge 0 Formula C10H18S InChIKeyhelp_outline FACAUSJJVBMWLV-JXMROGBWSA-N SMILEShelp_outline SC/C=C(/CCC=C(C)C)\C 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
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Namehelp_outline
5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA
Identifier
RHEA-COMP:15523
Reactive part
help_outline
- Name help_outline 5-methylaminomethyl-2-(Se-phospho)selenouridine 5'-monophosphate residue Identifier CHEBI:143702 Charge -2 Formula C11H15N3O10P2Se SMILEShelp_outline [C@@H]1(N2C(=NC(=O)C(=C2)C[NH2+]C)[Se]P([O-])(=O)[O-])O[C@H](COP(*)(=O)[O-])[C@H]([C@H]1O)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
Cross-references
RHEA:60172 | RHEA:60173 | RHEA:60174 | RHEA:60175 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Escherichia coli tRNA 2-selenouridine synthase (SelU) converts S2U-RNA to Se2U-RNA via S-geranylated-intermediate.
Sierant M., Leszczynska G., Sadowska K., Komar P., Radzikowska-Cieciura E., Sochacka E., Nawrot B.
To date the only tRNAs containing nucleosides modified with a selenium (5-carboxymethylaminomethyl-2-selenouridine and 5-methylaminomethyl-2-selenouridine) have been found in bacteria. By using tRNA anticodon-stem-loop fragments containing S2U, Se2U, or geS2U, we found that in vitro tRNA 2-selenou ... >> More
To date the only tRNAs containing nucleosides modified with a selenium (5-carboxymethylaminomethyl-2-selenouridine and 5-methylaminomethyl-2-selenouridine) have been found in bacteria. By using tRNA anticodon-stem-loop fragments containing S2U, Se2U, or geS2U, we found that in vitro tRNA 2-selenouridine synthase (SelU) converts S2U-RNA to Se2U-RNA in a two-step process involving S2U-RNA geranylation (with ppGe) and subsequent selenation of the resulting geS2U-RNA (with SePO<sub>3</sub><sup>3-</sup> ). No 'direct' S2U-RNA→Se2U-RNA replacement is observed in the presence of SelU/SePO<sub>3</sub><sup>3-</sup> only (without ppGe). These results suggest that the in vivo S2U→Se2U and S2U→geS2U transformations in tRNA, so far claimed to be the elementary reactions occurring independently in the same domain of the SelU enzyme, should be considered a combination of two consecutive events - geranylation (S2U→geS2U) and selenation (geS2U→Se2U). << Less
FEBS Lett. 592:2248-2258(2018) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
Comments
RHEA:60172 part of RHEA:42716