{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T02:48:02Z","timestamp":1772160482517,"version":"3.50.1"},"reference-count":43,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2006,4,4]],"date-time":"2006-04-04T00:00:00Z","timestamp":1144108800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Plant Journal"],"published-print":{"date-parts":[[2006,5]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    In this paper, we report the identification of genes from pine (\n                    <jats:italic>PpAAT<\/jats:italic>\n                    ), Arabidopsis (\n                    <jats:italic>AtAAT<\/jats:italic>\n                    ) and rice (\n                    <jats:italic>OsAAT<\/jats:italic>\n                    ) encoding a novel class of aspartate aminotransferase (AAT, EC 2.6.1.1) in plants. The enzyme is unrelated to other eukaryotic AATs from plants and animals but similar to bacterial enzymes. Phylogenetic analysis indicates that this prokaryotic\u2010type AAT is closely related to cyanobacterial enzymes, suggesting it might have an endosymbiotic origin. Interestingly, most of the essential residues involved in the interaction with the substrate and the attachment of pyridoxal phosphate cofactor in the active site of the enzyme were conserved in the deduced polypeptide. The polypeptide is processed\n                    <jats:italic>in planta<\/jats:italic>\n                    to a mature subunit of 45\u2003kDa that is immunologically distinct from the cytosolic, mitochondrial and chloroplastic isoforms of AAT previously characterized in plants. Functional expression of\n                    <jats:italic>PpAAT<\/jats:italic>\n                    sequences in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    showed that the processed precursor is assembled into a catalytically active homodimeric holoenzyme that is strictly specific for aspartate. These atypical genes are predominantly expressed in green tissues of pine, Arabidopsis and rice, suggesting a key role of this AAT in nitrogen metabolism associated with photosynthetic activity. Moreover, immunological analyses revealed that the plant prokaryotic\u2010type AAT is a nuclear\u2010encoded chloroplast protein. This implies that two plastidic AAT co\u2010exist in plants: a eukaryotic type previously characterized and the prokaryotic type described here. The respective roles of these two enzymes in plant amino acid metabolism are discussed.\n                  <\/jats:p>","DOI":"10.1111\/j.1365-313x.2006.02713.x","type":"journal-article","created":{"date-parts":[[2006,4,4]],"date-time":"2006-04-04T10:07:34Z","timestamp":1144145254000},"page":"414-425","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":55,"title":["Identification and functional analysis of a prokaryotic\u2010type aspartate aminotransferase: implications for plant amino acid metabolism"],"prefix":"10.1111","volume":"46","author":[{"given":"Fernando","family":"de la Torre","sequence":"first","affiliation":[]},{"given":"Laura De","family":"Santis","sequence":"additional","affiliation":[]},{"given":"Mar\u00eda Fernanda","family":"Su\u00e1rez","sequence":"additional","affiliation":[]},{"given":"Remedios","family":"Crespillo","sequence":"additional","affiliation":[]},{"given":"Francisco 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