InterPro domain: IPR003099

This entry represents prephenate dehydrogenase (PDHG) 1.3.1.12 , an enzyme involved in tyrosine biosynthesis [ 1 ] and related proteins.

Three enzymes catalyse the conversion of chorismate to hydroxyphenylpyruvate or pyruvate in the aromatic amino acid biosynthesis pathway. In this pathway, chorismate is a branch point intermediate that is converted to tryptophan, phenylalanine (Phe), and tyrosine (Tyr). In bacteria the enzymes, chorismate mutase (CM), prephenate dehydratase (PDT), and prephenate dehydrogenase (PDHG) are either present as distinct proteins or fusions combining two activities [ 2 ]. In the archaea Archaeoglobus fulgidus a single protein (AroQ) contains all three enzymatic domains [ 3 ].

This entry also matches 3-phosphoshikimate 1-carboxyvinyltransferase 2.5.1.19 .

1. Crystal structure of prephenate dehydrogenase from Streptococcus mutans. Int. J. Biol. Macromol. 49, 761-6
2. The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1317-25
3. Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus. Extremophiles 13, 191-8