{"entity": "publication", "iuid": "9b558221d00b4b45ad6db03f6f58941a", "timestamp": "2026-06-07T20:21:13.450Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/9b558221d00b4b45ad6db03f6f58941a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/9b558221d00b4b45ad6db03f6f58941a"}}, "title": "Unexpected Acetylation of Endogenous Aliphatic Amines by Arylamine N-Acetyltransferase NAT2.", "authors": [{"family": "Conway", "given": "Louis P", "initials": "LP"}, {"family": "Rendo", "given": "Veronica", "initials": "V", "orcid": "0000-0002-2983-4020", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9c4c9ca49eb64227be6574a4384ffb46.json"}}, {"family": "Correia", "given": "M\u00e1rio S P", "initials": "MSP", "orcid": "0000-0003-2125-4184", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d967f90e2be34feeae1b1fa84a9dbc83.json"}}, {"family": "Bergdahl", "given": "Ingvar A", "initials": "IA", "orcid": "0000-0003-1227-6859", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9a988c282ed84691bb8432f2ae4082df.json"}}, {"family": "Sj\u00f6blom", "given": "Tobias", "initials": "T", "orcid": "0000-0001-6668-4140", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/851b95a56b3244fb9bc7cec8294e7ae7.json"}}, {"family": "Globisch", "given": "Daniel", "initials": "D", "orcid": "0000-0002-4526-5788", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2cd75219d6894d6b851e202eaa40fc5f.json"}}], "type": "journal article", "published": "2020-08-17", "journal": {"title": "Angew. Chem. Int. Ed. Engl.", "issn": "1521-3773", "issn-l": "1433-7851", "volume": "59", "issue": "34", "pages": "14342-14346"}, "abstract": "N-Acetyltransferases play critical roles in the deactivation and clearance of xenobiotics, including clinical drugs. NAT2 has been classified as an arylamine N-acetyltransferase that mainly converts aromatic amines, hydroxylamines, and hydrazines. Herein, we demonstrate that the human arylamine N-acetyltransferase NAT2 also acetylates aliphatic endogenous amines. Metabolomic analysis and chemical synthesis revealed increased intracellular concentrations of mono- and diacetylated spermidine in human cell lines expressing the rapid compared to the slow acetylator NAT2 phenotype. The regioselective N8 -acetylation of monoacetylated spermidine by NAT2 answers the long-standing question of the source of diacetylspermidine. We also identified selective acetylation of structurally diverse alkylamine-containing drugs by NAT2, which may contribute to variations in patient responses. The results demonstrate a previously unknown functionality and potential regulatory role for NAT2, and we suggest that this enzyme should be considered for re-classification.", "doi": "10.1002/anie.202005915", "pmid": "32497306", "labels": {"Daniel Globisch": null, "SciLifeLab Fellow": null}, "xrefs": [{"db": "pmc", "key": "PMC7497018"}], "notes": [], "created": "2020-12-09T09:33:51.091Z", "modified": "2022-11-04T11:32:14.519Z"}