{"doi":"10.1128/mbio.00158-12","title":"PanM, an Acetyl-Coenzyme A Sensor Required for Maturation of\n            <scp>l</scp>\n            -Aspartate Decarboxylase (PanD)","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            Coenzyme A (CoA) is essential for cellular chemistry in all forms of life. The pantothenate moiety of CoA is generated from the condensation of pantoate and β-alanine. β-Alanine is formed by decarboxylation of\n            <jats:sc>l</jats:sc>\n            -aspartate catalyzed by PanD, a pyruvoyl enzyme that is synthesized by the cell as an inactive precursor (pro-PanD). Maturation of pro-PanD into PanD occurs via a self-cleavage event at residue Ser25, which forms the catalytic pyruvoyl moiety. We recently reported that\n            <jats:named-content content-type=\"genus-species\">Salmonella enterica</jats:named-content>\n            PanM was necessary for pro-PanD maturation, both\n            <jats:italic>in vitro</jats:italic>\n            and\n            <jats:italic>in vivo</jats:italic>\n            . Notably, PanM is annotated as a Gcn5-like\n            <jats:italic>N</jats:italic>\n            -acetyltransferase (GNAT), which suggested that lysine acetylation might be part of the mechanism of maturation. Here we show that PanM lacks acetyltransferase activity and that acetyl-CoA stimulates its activity. Results of experiments with nonhydrolyzable ethyl-CoA and genetically encoded acetyl-lysine-containing PanD support the conclusion that PanM-dependent pro-PanD maturation does not involve an acetyl transfer event. We also show that CoA binding to PanM is needed for\n            <jats:italic>in vivo</jats:italic>\n            activity and that disruption of CoA binding prevents PanM from interacting with PanD. We conclude that PanM is a GNAT homologue that lost its acetyltransferase activity and evolved a new function as an acetyl-CoA sensor that can trigger the maturation of pro-PanD.\n          </jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE</jats:bold>\n            Nε-lysine acetylation is increasingly being recognized as a widespread and important form of posttranslational regulation in bacteria. The acetyltransferases that catalyze these reactions are poorly characterized in bacteria. Based on annotation, most bacterial genomes contain several acetyltransferases, but the physiological roles of only a handful have been determined. Notably, a subset of putative acetyltransferases lack residues that are critical for activity in most biochemically characterized acetyltransferases. We show that one such putative acetyltransferase, PanM (formerly YhhK), lacks acetyltransferase activity but functions instead as an acetyl-coenzyme A (CoA) sensor. This work establishes the possibility that, like PanM, other putative acetyltransferases may have evolved new functions while retaining the ability to sense acetyl-CoA.\n          </jats:p>","journal":"mBio","year":2012,"id":14583,"datarank":1.1767739206424044,"base_score":2.833213344056216,"endowment":2.833213344056216,"self_citation_contribution":0.42498200160843247,"citation_network_contribution":0.7517919190339718,"self_endowment_contribution":0.42498200160843247,"citer_contribution":0.7517919190339718,"corpus_percentile":null,"corpus_rank":null,"citation_count":16,"citer_count":14,"citers_with_citation_signal":13,"citers_with_endowment":13,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":114511,"name":"Alex C. Tucker","orcid":"0000-0002-9307-7204","position":1,"is_corresponding":false},{"id":114502,"name":"Jorge C. Escalante-Semerena","orcid":null,"position":2,"is_corresponding":false},{"id":114574,"name":"Tara N. Stuecker","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":2.833213344056216,"endowment":2.833213344056216,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22782525","pmcid":"PMC3398536","openalex_id":"https://openalex.org/W2163363144","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM062203","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"T32-GM07215","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"T32 GM007215","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01-GM62203","title":null},{"funder_name":"National Institutes of Health","grant_id":"2T32GM007215-36","title":"Graduate Training in Molecular Biosciences"},{"funder_name":"National Institutes of Health","grant_id":"5R01GM062203-06","title":"Sirtuins and Metabolic Pathway Integration"}],"total_grants":6,"fwci":0.8026,"citation_percentile":0.77117205,"influential_citations":2,"citation_trend":[{"year":2012,"count":1},{"year":2015,"count":3},{"year":2016,"count":2},{"year":2017,"count":2},{"year":2018,"count":1},{"year":2020,"count":1},{"year":2022,"count":1},{"year":2023,"count":1},{"year":2025,"count":4}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.1128/mbio.00158-12","host_type":"journal"},{"url":"https://doi.org/10.1128/mbio.00158-12","host_type":"GOLD"},{"url":"https://doi.org/10.1128/mbio.00158-12","host_type":"publisher"},{"url":"https://journals.asm.org/doi/pdf/10.1128/mBio.00158-12","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22782525","host_type":"repository"},{"url":"https://doaj.org/article/37b66fd3b45c48d3b49b3323dd2c453a","host_type":"repository"},{"url":"https://doaj.org/article/925eaabd644d459f9b33c1412c9e9b91","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3398536","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC3398536","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC3398536?pdf=render","host_type":"Europe_PMC"},{"url":"https://mbio.asm.org/content/3/4/e00158-12.full.pdf","host_type":""},{"url":"http://dx.doi.org/10.1128/mBio.00158-12","host_type":""},{"url":"https://dx.doi.org/10.1128/mbio.00158-12","host_type":""}],"fields_of_study":["Neurological diseases and metabolism","Porphyrin Metabolism and Disorders","Biotin and Related Studies","Medicine","Biology","Chemistry","0301 basic medicine","03 medical and health sciences","Acetyl Coenzyme A","Acetyltransferases","Amino Acid Sequence","Bacterial Proteins","Binding Sites","Carboxy-Lyases","Gene Expression Regulation, Enzymologic","Models, Molecular","Molecular Sequence Data","Protein Binding","Salmonella typhimurium","Sequence Alignment"],"mesh_terms":["Acetyl Coenzyme A","Acetyltransferases","Amino Acid Sequence","Bacterial Proteins","Binding Sites","Carboxy-Lyases","Models, Molecular","Molecular Sequence Data","Protein Binding","Salmonella typhimurium","Gene Expression Regulation, Enzymologic","Sequence Alignment"],"keywords":["Acetyltransferase","Acetylation","Acetyl-CoA","Coenzyme A","Acetyltransferases","Biochemistry","Lysine","Enzyme","Biology","Moiety","Chemistry","Amino acid","Stereochemistry","Gene","Models, Molecular","Salmonella typhimurium","Binding Sites","Carboxy-Lyases","Molecular Sequence Data","Microbiology","QR1-502","Gene Expression Regulation, Enzymologic","Bacterial Proteins","Acetyl Coenzyme A","Amino Acid Sequence","Sequence Alignment","Research Article","Protein Binding"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-01T12:28:43.670592Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}