Prephenate dehydrogenase, fungal
InterPro Protein Domain record
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description
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<p>Members of this group catalyse a step in tyrosine biosynthesis in the shikimate pathway, which is present only in bacteria, archaea, fungi, and plants [<cite idref="PUB00015637"/>]. They belong to the prephenate dehydrogenase (PDH) domain superfamily <db_xref db="INTERPRO" dbkey="IPR003099"/>, (for more information see also <db_xref db="INTERPRO" dbkey="IPR008235"/>, <db_xref db="INTERPRO" dbkey="IPR008236"/>, <db_xref db="INTERPRO" dbkey="IPR008299"/>, <db_xref db="INTERPRO" dbkey="IPR008244"/>, <db_xref db="INTERPRO" dbkey="IPR012070"/> etc).</p> <p>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 [<cite idref="PUB00011046"/>, <cite idref="PUB00016002"/>]. Prephenate dehydrogenase (PDH) (<db_xref db="EC" dbkey="1.3.1.12"/>, <db_xref db="EC" dbkey="1.3.1.13"/>) catalyses oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate. Arogenate dehydrogenase (<db_xref db="EC" dbkey="1.3.1.43"/>) 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 [<cite idref="PUB00011044"/>].</p> <p>This group represents fungal PDH enzymes. It is closely related to the plant group (<db_xref db="INTERPRO" dbkey="IPR012070"/>), 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 [<cite idref="PUB00016053"/>, <cite idref="PUB00015943"/>]. </p>
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Prephenate dehydrogenase, fungal
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