| Type: | Conserved_site | Name: | Prephenate dehydratase, conserved site |
| Description: | Prephenate dehydratase (, PDT) catalyses the decarboxylation of prephenate to phenylpyruvate. In microorganisms it is part of the terminal pathway of phenylalanine biosynthesis. In some bacteria such as Escherichia coliPDT is part of a bifunctional enzyme (P-protein) that also catalyses the transformation of chorismate into prephenate (chorismate mutase, , ) while in other bacteria it is a monofunctional enzyme. In the archaea Archaeoglobus fulgidus is part of a trifunctional enzyme []. The sequence of monofunctional PDT aligns well with the C-terminal part of P-proteins [].This entry represents two conserved regions. The first contains a conserved threonine which appears to be essential for the activity of the enzyme in E. coli []. The second region is located in the regulatory (Phe binding) region in the part C-terminal to PDT and this includes a conserved glutamate. | Short Name: | Preph_deHydtase_CS |
