EC Number   |
General Information |
Reference |
|---|
   1.3.1.78 | evolution |
prephenate dehydrogenases (TyrAps, also known as PDHs) from two legumes, Glycine max (soybean) and Medicago truncatula, are phylogenetically distinct from canonical plant ADH enzymes, prefer prephenate to arogenate substrate, localize outside of the plastids and are not inhibited by L-Tyr. Diversification of primary metabolic Tyr pathway via an alternative cytosolic PDH pathway in plants, phylogenetic and biochemical differentiation of ADHs and PDHs |
745837 |
| 1.3.1.78 | malfunction |
TyrA1 suppression reduces seed yield due to impaired anther dehiscence |
763581 |
| 1.3.1.78 | malfunction |
TyrA2 knockout leads to slow growth with reticulate leaves. TyrA2 deficiency alters the levels of multiple amino acids but not of tyrosine |
763581 |
| 1.3.1.78 | metabolism |
in plants, L-Tyr is synthesized in the plastids via the arogenate dehydrogenase pathway, in which prephenate is first converted to arogenate by prephenate aminotransferase, EC 2.6.1.7, and then to L-Tyr by enzyme ADH |
745837 |
| 1.3.1.78 | metabolism |
most plants synthesize tyrosine by TyrA arogenate dehydrogenases. TyrA1 and TyrA2 have distinct and overlapping functions in flower and leaf development, respectively. The imbalance of tyrosine, caused by altered TyrA activity and regulation, impacts growth and development of Arabidopsis |
763581 |
