{"doi":"10.1038/s41598-017-13897-w","title":"Site-specific and kinetic characterization of enzymatic and nonenzymatic protein acetylation in bacteria","abstract":"<jats:title>Abstract</jats:title><jats:p>Reversible N<jats:sup>ε</jats:sup>-lysine acetylation has emerging as an important metabolic regulatory mechanism in microorganisms. Herein, we systematically investigated the site-specific and kinetic characterization of enzymatic (lysine acetyltransferase) and nonenzymatic acetylation (AcP-dependent or Acyl-CoA-dependent), as well as their different effect on activity of metabolic enzyme (AMP-forming acetyl-CoA synthetase, Acs). It was found that <jats:italic>Bacillus subtilis</jats:italic> acetyl-CoA synthetase (<jats:italic>Bs</jats:italic>AcsA) can be acetylated <jats:italic>in vitro</jats:italic> either catalytically by lysine acetyltransferase <jats:italic>Bs</jats:italic>AcuA and Ac-CoA (at low concentration), or nonenzymatically by Ac-CoA or AcP (at high concentration). Two distinct mechanisms show preference for different lysine acetylation site (enzymatic acetylation for K549 and nonenzymatic acetylation for K524), and reveal different dynamics of relative acetylation changes at these lysine sites. The results demonstrated that lysine residues on the same protein exhibit different acetylation reactivity with acetyl-phosphate and acetyl-CoA, which was determined by surface accessibility, three-dimensional microenvironment, and pKa value of lysine. Acetyl-CoA synthetase is inactivated by AcuA-catalyzed acetylation, but not by nonenzymatic acetylation.</jats:p>","journal":"Scientific Reports","year":2017,"id":14586,"datarank":1.489450556382676,"base_score":3.713572066704308,"endowment":3.713572066704308,"self_citation_contribution":0.5570358100056463,"citation_network_contribution":0.9324147463770298,"self_endowment_contribution":0.5570358100056463,"citer_contribution":0.9324147463770298,"corpus_percentile":null,"corpus_rank":null,"citation_count":40,"citer_count":37,"citers_with_citation_signal":33,"citers_with_endowment":33,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":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":114499,"name":"Di You","orcid":null,"position":1,"is_corresponding":false},{"id":114503,"name":"Bang-Ce Ye","orcid":"0000-0002-5555-5359","position":2,"is_corresponding":false},{"id":114579,"name":"Miao-Miao Wang","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.713572066704308,"endowment":3.713572066704308,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"29093482","pmcid":"PMC5665961","openalex_id":"https://openalex.org/W2765592108","authors":[],"funders":[],"total_grants":0,"fwci":1.1552,"citation_percentile":0.7665712,"influential_citations":0,"citation_trend":[{"year":2018,"count":2},{"year":2019,"count":5},{"year":2020,"count":3},{"year":2021,"count":3},{"year":2022,"count":6},{"year":2023,"count":8},{"year":2024,"count":10},{"year":2025,"count":3}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://www.nature.com/articles/s41598-017-13897-w.pdf","host_type":"journal"},{"url":"https://www.nature.com/articles/s41598-017-13897-w.pdf","host_type":"GOLD"},{"url":"https://www.nature.com/articles/s41598-017-13897-w.pdf","host_type":"publisher"},{"url":"https://www.nature.com/articles/s41598-017-13897-w","host_type":"publisher"},{"url":"https://doi.org/10.1038/s41598-017-13897-w","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/29093482","host_type":"repository"},{"url":"https://doaj.org/article/6fc038c38842494586d15c457e735a4a","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/5665961","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC5665961","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC5665961?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Enzyme Structure and Function","Protein Structure and Dynamics","Biochemical and Molecular Research","Biology","Chemistry","Acetate-CoA Ligase","Acetyl Coenzyme A","Acetylation","Bacillus subtilis","Escherichia coli","Escherichia coli Proteins","Lysine Acetyltransferases","Protein Processing, Post-Translational"],"mesh_terms":["Lysine Acetyltransferases","Acetyl Coenzyme A","Acetate-CoA Ligase","Acetylation","Bacillus subtilis","Escherichia coli","Protein Processing, Post-Translational","Escherichia coli Proteins"],"keywords":["Acetylation","Lysine","Acetyltransferase","Biochemistry","Enzyme","Acetyl-CoA","Chemistry","Bacillus subtilis","Amino acid","Biology","Bacteria","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-01T12:32:10.775675Z","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":[]}