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In enzymology, an arogenate dehydrogenase (EC 1.3.1.79) is an enzyme that catalyzes the chemical reaction

L-arogenate + NAD(P)+ ${\displaystyle \rightleftharpoons }$ L-tyrosine + NAD(P)H + CO₂

The 3 substrates of this enzyme are L-arogenate, NAD, and NADP, whereas its 4 products are L-tyrosine, NADH, NADPH, 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(P)+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, and pretyrosine dehydrogenase (ambiguous).

References

• Connelly JA, Conn EE (1986). "Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase". Z. Naturforsch. C. 41 (1–2): 69–78. doi:10.1515/znc-1986-1-212. PMID 2939643.
• Bonner C, Jensen R (1987). "Arogenate dehydrogenase". Metabolism of Aromatic Amino Acids and Amines. Methods in Enzymology. Vol. 142. pp. 488–94. doi:10.1016/S0076-6879(87)42060-0. ISBN 978-0-12-182042-8. PMID 3600376.

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