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Arogenate dehydrogenase
・ Arogenate dehydrogenase (NAD(P)+)
・ Arogenate dehydrogenase (NADP+)
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Arogenate dehydrogenase : ウィキペディア英語版
Arogenate dehydrogenase

In enzymology, an arogenate dehydrogenase () is an enzyme that catalyzes the chemical reaction
:L-arogenate + NAD+ \rightleftharpoons L-tyrosine + NADH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NAD+, whereas its 3 products are L-tyrosine, NADH, and CO2.
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.
==Structural studies==

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .

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