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Literature summary extracted from

  • de la Torre, F.; El-Azaz, J.; Avila, C.; Canovas, F.M.
    Deciphering the role of aspartate and prephenate aminotransferase activities in plastid nitrogen metabolism (2014), Plant Physiol., 164, 92-104.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.6.1.78 plastid
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 Nicotiana benthamiana 9536
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2.6.1.79 plastid
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 Nicotiana benthamiana 9536
-

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.78 Nicotiana benthamiana
-
-
-
2.6.1.79 Nicotiana benthamiana
-
-
-

General Information

EC Number General Information Comment Organism
2.6.1.78 physiological function suppression of prephenate aminotransferase leads to a severe reduction in growth and strong chlorosis symptoms. Prephenate aminotransferase silenced plants exhibit extremely reduced levels of asparagine and are greatly affected in their phenylalanine metabolism and lignin deposition. Prephenate aminotransferase suppression triggers a transcriptional reprogramming in plastid nitrogen metabolism. The enzyme is essential for plant growth and development Nicotiana benthamiana
2.6.1.79 physiological function suppression of prephenate aminotransferase leads to a severe reduction in growth and strong chlorosis symptoms. Prephenate aminotransferase silenced plants exhibit extremely reduced levels of asparagine and are greatly affected in their phenylalanine metabolism and lignin deposition. Prephenate aminotransferase suppression triggers a transcriptional reprogramming in plastid nitrogen metabolism. The enzyme is essential for plant growth and development Nicotiana benthamiana