In enzymology, arogenate dehydrogenase () is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-arogenic acid (shown as its conjugate base arogenate) and oxidised nicotinamide adenine dinucleotide (NAD<sup>+</sup>). Its products are L-tyrosine, reduced NADH, and carbon dioxide.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, pretyrosine dehydrogenase (ambiguous), and L-arogenate:NAD+ oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .