Enzymes
| UniProtKB help_outline | 6,429 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
cytidine34 in elongator tRNAMet
Identifier
RHEA-COMP:10693
Reactive part
help_outline
- Name help_outline CMP residue Identifier CHEBI:82748 Charge -1 Formula C9H11N3O7P Positionhelp_outline 34 SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])(-*)=O)[C@@H](O-*)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 66 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetate Identifier CHEBI:30089 (CAS: 71-50-1) help_outline Charge -1 Formula C2H3O2 InChIKeyhelp_outline QTBSBXVTEAMEQO-UHFFFAOYSA-M SMILEShelp_outline CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 180 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,284 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N4-acetylcytidine34 in elongator tRNAMet
Identifier
RHEA-COMP:10694
Reactive part
help_outline
- Name help_outline N4-acetylcytidine 5'-phosphate residue Identifier CHEBI:74900 Charge -1 Formula C11H13N3O8P Positionhelp_outline 34 SMILEShelp_outline C1=CC(=NC(N1[C@@H]2O[C@H](COP(*)(=O)[O-])[C@H]([C@H]2O)O*)=O)NC(C)=O 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 AMP Identifier CHEBI:456215 Charge -2 Formula C10H12N5O7P InChIKeyhelp_outline UDMBCSSLTHHNCD-KQYNXXCUSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 512 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,139 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:58144 | RHEA:58145 | RHEA:58146 | RHEA:58147 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Publications
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Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis.
Taniguchi T., Miyauchi K., Sakaguchi Y., Yamashita S., Soma A., Tomita K., Suzuki T.
Modification of tRNA anticodons plays a critical role in ensuring accurate translation. N<sup>4</sup>-acetylcytidine (ac<sup>4</sup>C) is present at the anticodon first position (position 34) of bacterial elongator tRNA<sup>Met</sup>. Herein, we identified Bacillus subtilis ylbM (renamed tmcAL) as ... >> More
Modification of tRNA anticodons plays a critical role in ensuring accurate translation. N<sup>4</sup>-acetylcytidine (ac<sup>4</sup>C) is present at the anticodon first position (position 34) of bacterial elongator tRNA<sup>Met</sup>. Herein, we identified Bacillus subtilis ylbM (renamed tmcAL) as a novel gene responsible for ac<sup>4</sup>C34 formation. Unlike general acetyltransferases that use acetyl-CoA, TmcAL activates an acetate ion to form acetyladenylate and then catalyzes ac<sup>4</sup>C34 formation through a mechanism similar to tRNA aminoacylation. The crystal structure of TmcAL with an ATP analog reveals the molecular basis of ac<sup>4</sup>C34 formation. The ΔtmcAL strain displayed a cold-sensitive phenotype and a strong genetic interaction with tilS that encodes the enzyme responsible for synthesizing lysidine (L) at position 34 of tRNA<sup>Ile</sup> to facilitate AUA decoding. Mistranslation of the AUA codon as Met in the ΔtmcAL strain upon tilS repression suggests that ac<sup>4</sup>C34 modification of tRNA<sup>Met</sup> and L34 modification of tRNA<sup>Ile</sup> act cooperatively to prevent misdecoding of the AUA codon. << Less
Nat. Chem. Biol. 14:1010-1020(2018) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
Multi-step reaction: RHEA:58136 and RHEA:58140