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Unlike other insect AASs that convert Dopa, PonAAS2 uniquely converts l-tryptophan (Trp) into indole-3-acetaldehyde, a precursor of IAA. In this study, an examination of AAS enzymes from various insect species revealed that the ability to convert Trp has been acquired in only a very limited taxonomic group. Comparative analysis between PonAAS2 and DjAAS2 from a gall wasp showed that, despite having conserved substrate-recognizing amino acids, they exhibit different substrate specificities. This difference likely arises from variations in how these enzymes\u2019 monomers interact during dimer formation, as demonstrated by amino acid substitution experiments and structural predictions.<\/jats:p>","DOI":"10.1093\/bbb\/zbaf005","type":"journal-article","created":{"date-parts":[[2025,1,17]],"date-time":"2025-01-17T05:20:41Z","timestamp":1737091241000},"page":"533-540","source":"Crossref","is-referenced-by-count":1,"title":["A unique substrate specificity of PonAAS2, an aromatic aldehyde synthase, involved in phytohormone auxin biosynthesis in a gall-inducing sawfly <i>Euura<\/i> sp. \u201c<i>Pontania<\/i>\u201d"],"prefix":"10.1093","volume":"89","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4574-9504","authenticated-orcid":false,"given":"Yoshihito","family":"Suzuki","sequence":"first","affiliation":[{"name":"Department of Food and Life Sciences, College of Agriculture, Ibaraki University , Ibaraki ,","place":["Japan"]},{"name":"United Graduate School of Agricultural 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