1 Found In
| DB identifier | Type | Name |
|---|---|---|
| IPR008242 | Family | Bifunctional P-protein, chorismate mutase/prephenate dehydratase |
| Type: | Domain | Name: | Prephenate dehydratase |
| 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 [].The prephenate dehydratase domain is also found in the six PDT-like homologues of Arabidopsis. They use arogenate more efficiently than prephenate, and consequently they have been classified as arogenate dehydratases []. | Short Name: | Preph_deHydtase |
| DB identifier | Type | Name |
|---|---|---|
| IPR008242 | Family | Bifunctional P-protein, chorismate mutase/prephenate dehydratase |
