LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | 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 coli PDT 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 |
