In bacteria and plants, the first enzyme of the shikimate pathway, DAHP3 synthase (EC 4.1.2.15), catalyzes the condensation ofphosphoenolpyruvate and erythrose-4-phosphate to form DAHP and Pi ( 11, 2 1). The role of this enzyme as an important regulator has been clearly demonstrated in bacteria, where modulation of the enzyme activity by feedback inhibition is the major mechanism to control carbon flow into the shikimate pathway (18). The aromatic amino acids phenylalanine, tyrosine, and tryptophan serve as specific inhibitors for three different isoenzymes encoded by three separate genes (11,21).In plants, the shikimate pathway provides the precursors not only for the synthesis of the aromatic amino acids but also for a variety of derived secondary metabolites, such as lignins, alkaloids, and flavonoids (9). Plant DAHP synthases are not inhibited by the aromatic amino acids (20, 28), but two DAHP synthase isoenzymes are distinguishable through their metal requirements and their sensitivity to various metabolic intermediates in a variety ofplants (8). DAHP synthase-