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 | Domain |
| 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 [].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 |
