InterPro domain: IPR001086

Prephenate dehydratase ( 4.2.1.51 , 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, IPR002701 , 5.4.99.5 ) while in other bacteria it is a monofunctional enzyme. In the archaea Archaeoglobus fulgidus is part of a trifunctional enzyme [ 1 ]. The sequence of monofunctional PDT aligns well with the C-terminal part of P-proteins [ 2 ].

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 [ 3 ].

1. Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus. Extremophiles 13, 191-8
2. Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase. J. Biol. Chem. 273, 17012-7
3. Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and characterization of arogenate dehydratases. J. Biol. Chem. 282, 30827-35