Journal
FEBS LETTERS
Volume 584, Issue 20, Pages 4357-4360Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.09.037
Keywords
Aspartate aminotransferase; Aromatic amino acid; Enzymology; Metabolism; Plant; Prephenate aminotransferase
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In all organisms synthesising phenylalanine and/or tyrosine via arogenate, a prephenate aminotransferase is required for the transamination of prephenate into arogenate. The identity of the gene encoding this enzyme in the organisms where this activity occurs is still unknown. Glutamate/aspartate-prephenate aminotransferase (PAT) is thus the last homeless enzyme in the aromatic amino acids pathway. We report on the purification, mass spectrometry identification and biochemical characterization of Arabidopsis thaliana prephenate aminotransferase. Our data revealed that this activity is housed by the prokaryotic-type plastidic aspartate aminotransferase (At2g22250). This represents the first identification of a gene encoding PAT. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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