| Type: | Family | Name: | Prephenate dehydrogenase, fungal |
| 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 , (for more information see also , , , , etc).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 [, ]. | Short Name: | Prephenate_DH_fun |
