Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049359 | FEBS Letters | 2010 | 4 Pages |
Abstract
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.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Matthieu Graindorge, Cécile Giustini, Anne Claire Jacomin, Alexandra Kraut, Gilles Curien, Michel Matringe,