{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tabagari N"],"funding":["European Research Council"],"pagination":["100132"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12268091"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12"],"pubmed_abstract":["Proteins are heteropolymers composed of twenty standard amino acids, but over 500 non-proteogenic amino acids exist in nature that can be misincorporated into proteins. Canavanine is an antimetabolite of the chemically similar L-arginine. It can be utilized by bacteria such as <i>Pseudomonas canavaninivorans</i> in the legume rhizome as a sole source of carbon and nitrogen. However, canavanine misincorporates in proteins of this bacterium as its arginyl-tRNA synthetase loads tRNA<sup>Arg</sup> with both canavanine and arginine. Canavanyl-tRNA<sup>Arg</sup> deacetylase (CtdA) removes canavanine from misloaded tRNA<sup>Arg</sup>, preventing its protein toxicity, being the first enzyme known to edit tRNA mischarged with a non-proteinogenic amino acid. We have elucidated CtdA's crystal structu"],"journal":["Journal of structural biology: X"],"pubmed_title":["Indel-driven evolution of the canavanine tRNA-editing deacetylase enzyme CtdA."],"pmcid":["PMC12268091"],"funding_grant_id":["681777"],"pubmed_authors":["Hartig JS","Hauth F","Mayans O","Tabagari N","Fleming JR"],"additional_accession":[]},"is_claimable":false,"name":"Indel-driven evolution of the canavanine tRNA-editing deacetylase enzyme CtdA.","description":"Proteins are heteropolymers composed of twenty standard amino acids, but over 500 non-proteogenic amino acids exist in nature that can be misincorporated into proteins. Canavanine is an antimetabolite of the chemically similar L-arginine. It can be utilized by bacteria such as <i>Pseudomonas canavaninivorans</i> in the legume rhizome as a sole source of carbon and nitrogen. However, canavanine misincorporates in proteins of this bacterium as its arginyl-tRNA synthetase loads tRNA<sup>Arg</sup> with both canavanine and arginine. Canavanyl-tRNA<sup>Arg</sup> deacetylase (CtdA) removes canavanine from misloaded tRNA<sup>Arg</sup>, preventing its protein toxicity, being the first enzyme known to edit tRNA mischarged with a non-proteinogenic amino acid. We have elucidated CtdA's crystal structu","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-03-16T07:55:15.327Z","creation":"2025-08-15T03:06:27.968Z"},"accession":"S-EPMC12268091","cross_references":{"pubmed":["40687620"],"doi":["10.1016/j.yjsbx.2025.100132"]}}