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In this work, the structural and functional properties of plant N\u2010acetylornithine glutamate acetyltransferase (NAOGAT), the key deacetylating enzyme of the cyclic ornithine pathway and the target of mangotoxin, were investigated. We determined the structures of rice and maize NAOGATs to near\u2010atomic resolution. Plant NAOGATs demonstrate a characteristic ArgJ\u2010like N\u2010terminal nucleophile fold, undergoing autoproteolytic maturation into \u03b1 and \u03b2 subunits, generating an active\u2010site threonine nucleophile at the N\u2010terminus of the \u03b2\u2010chain. The enzyme catalyses acetyl transfer via a bi\u2010bi ping\u2013pong mechanism in a bidirectional manner, although the acetylornithine\u2010to\u2010acetylglutamate conversion is preferred. NAOGAT undergoes minimal structural rearrangements during the reaction, however threonine acetylation causes pronounced changes in electrostatic potential around the active site which is also exhibited by the increased NAOGAT stability in the thermal shift assay. We did not detect clear evidence of NAOGAT acetylation by acetylCoA in our structural and biophysical data, which supports the specialisation of plant NAOGATs towards acetylornithine\u2010glutamate transacetylation. Finally, predictive bioinformatic analysis of the\n                    <jats:italic>P. syringae<\/jats:italic>\n                    mangotoxin\u2010producing operon, in the context of NAOGAT architecture, provided a basis for potential structural features of mangotoxin.\n                  <\/jats:p>","DOI":"10.1111\/pce.70891","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T13:42:43Z","timestamp":1789998163000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Plant NAOGAT (ArgJ) Structure Reveals Mechanism of Ornithine Biosynthesis, Preference for Acetylornithine and Susceptibility to Mangotoxin"],"prefix":"10.1111","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6996-3783","authenticated-orcid":false,"given":"Maciej","family":"Nielipinski","sequence":"first","affiliation":[{"name":"Institute of Molecular and Industrial Biotechnology, Faculty of Biotechnology and Food Sciences Lodz University of Technology \u0141\u00f3d\u017a Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1565-7307","authenticated-orcid":false,"given":"Agnieszka J.","family":"Pietrzyk\u2010Brzezinska","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Industrial Biotechnology, Faculty of Biotechnology and Food Sciences Lodz University of Technology \u0141\u00f3d\u017a Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2532-5672","authenticated-orcid":false,"given":"Aleksandra","family":"Twarda\u2010Clapa","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Industrial Biotechnology, Faculty of Biotechnology and Food Sciences Lodz University of Technology \u0141\u00f3d\u017a Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4008-4360","authenticated-orcid":false,"given":"Bartosz","family":"Sekula","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Industrial Biotechnology, Faculty of Biotechnology and Food Sciences Lodz University of Technology \u0141\u00f3d\u017a 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