{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Haas D"],"funding":["National Science Foundation"],"pagination":["e0163022"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9426524"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(4)"],"pubmed_abstract":["Analysis of the genes retained in the minimized <i>Mycoplasma</i> JCVI-Syn3A genome established that systems that repair or preempt metabolite damage are essential to life. Several genes known to have such functions were identified and experimentally validated, including 5-formyltetrahydrofolate cycloligase, coenzyme A (CoA) disulfide reductase, and certain hydrolases. Furthermore, we discovered that an enigmatic YqeK hydrolase domain fused to NadD has a novel proofreading function in NAD synthesis and could double as a MutT-like sanitizing enzyme for the nucleotide pool. Finally, we combined metabolomics and cheminformatics approaches to extend the core metabolic map of JCVI-Syn3A to include promiscuous enzymatic reactions and spontaneous side reactions. This extension revealed that sever"],"journal":["mBio"],"pubmed_title":["Metabolite Damage and Damage Control in a Minimal Genome."],"pmcid":["PMC9426524"],"funding_grant_id":["MCB-1840320","MCB-1611846","MCB-1611952","MCB-1818344","MCB-1611711","MCB-1840301"],"pubmed_authors":["Kurilyak I","Glass JI","Lerma-Ortiz C","Folz J","Henry CS","Bruner SD","Wise KS","Brown G","Huang L","Hanson AD","Haas D","Sun L","Beaudoin GAW","de Crecy-Lagard V","Luthey-Schulten Z","Wilson MA","Fiehn O","Breuer M","Yakunin AF","Lin J","Thamm AM","Sun J"],"additional_accession":[]},"is_claimable":false,"name":"Metabolite Damage and Damage Control in a Minimal Genome.","description":"Analysis of the genes retained in the minimized <i>Mycoplasma</i> JCVI-Syn3A genome established that systems that repair or preempt metabolite damage are essential to life. Several genes known to have such functions were identified and experimentally validated, including 5-formyltetrahydrofolate cycloligase, coenzyme A (CoA) disulfide reductase, and certain hydrolases. Furthermore, we discovered that an enigmatic YqeK hydrolase domain fused to NadD has a novel proofreading function in NAD synthesis and could double as a MutT-like sanitizing enzyme for the nucleotide pool. Finally, we combined metabolomics and cheminformatics approaches to extend the core metabolic map of JCVI-Syn3A to include promiscuous enzymatic reactions and spontaneous side reactions. This extension revealed that sever","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-05-29T16:11:40.099Z","creation":"2025-04-04T09:32:32.5Z"},"accession":"S-EPMC9426524","cross_references":{"pubmed":["35862786"],"doi":["10.1128/mbio.01630-22"]}}