Prephenate dehydrogenase/arogenate dehydrogenase
InterPro Protein Domain record
-
description
-
-
<p>Members of this group catalyse a step in tyrosine biosynthesis in the shikimate pathway, which is present only in bacteria, fungi, and plants. They contain both a prephenate dehydrogenase domain (PDH) and a regulatory domain. </p> <p>Prephenate dehydrogenase (PDH) (<db_xref db="EC" dbkey="1.3.1.12"/>) catalyses oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate. Many of the proteins containing this domain are able to use the alternative intermediates of tyrosine biosynthesis, prephenate or L-arogenate, as substrates, and thus contain both prephenate dehydrogenase and arogenate dehydrogenase activities (arogenate dehydrogenase, <db_xref db="EC" dbkey="1.3.1.43"/> catalyses oxidative decarboxylation of arogenate into tyrosine). Therefore, they are also called cyclohexadienyl dehydrogenases. Please see related groups (e.g. <db_xref db="INTERPRO" dbkey="IPR008235"/>) for additional information on prephenate dehydrogenases.</p> <p>The C-terminal domain of these proteins is predicted to play a regulatory role. It has a distant but unmistakable similarity to the ferredoxin-fold anticodon-binding domain found in some phenylalanyl-tRNA synthetases (detected by PSI-BLAST). There is evidence that the dehydrogenase activity of chorismate mutase-prephenate dehydrogenase, the allosteric enzyme of the tyrosine biosynthetic pathway in <taxon tax_id="562">Escherichia coli</taxon>, is inhibited by tRNA. Related prephenate dehydrogenases from yeast and plants (e.g., S46037) do not have this domain and instead have a different domain at the C terminus.</p> <p>For additional information please see [<cite idref="PUB00011066"/>, <cite idref="PUB00011045"/>].</p>
-
label
-
-
Prephenate dehydrogenase/arogenate dehydrogenase
-
attributionURL
-
-
signatures_SMART
-
-
type
-
-
seeAlso
-
-
children
-
-
contains
-
-
PDB_structure
-