| Description | Members of this group catalyse a step in tyrosine biosynthesis in the shikimate pathway, which is present only in bacteria, archaea, fungi, and plants [ ]. They belong to the prephenate dehydrogenase (PDH) domain superfamily . Many of the PDH enzymes are able to use the alternative intermediates of tyrosine biosynthesis, prephenate or L-arogenate, as substrates, having both prephenate dehydrogenase and arogenate dehydrogenase activities, and are sometimes collectively called cyclohexadienyl dehydrogenases [ , ]. Prephenate dehydrogenase (PDH) (, ) catalyses oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate. Arogenate dehydrogenase ( ) catalyses oxidative decarboxylation of arogenate into tyrosine. The existence of different combinations for routing prephenate to phenylalanine or tyrosine means that the substrate specificity of a particular enzyme (arogenate or prephenate), as well as its susceptibility to feedback regulation by different metabolites is not easily predictable, and must be experimentally studied in detail [ ].This group represents fungal PDH enzymes. It is closely related to the plant group ( ), but is characterised by the unique C-terminal domain found only in the fungal enzymes. The experimentally characterised yeast enzyme is a NAD-dependent prephenate dehydrogenase [ , ]. | Name | Prephenate dehydrogenase, fungal |
| Short Name | Prephenate_DH_fun | Type | Family |
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