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In enzymology, an arogenate dehydrogenase (NADP+) ( EC 1.3.1.78) is an enzyme that catalyzes the chemical reaction

L-arogenate + NADP⁺ ${\displaystyle \rightleftharpoons }$ L-tyrosine + NADPH + CO₂

Thus, the two substrates of this enzyme are L-arogenate and NADP⁺, whereas its 3 products are L-tyrosine, 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:NADP+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), pretyrosine dehydrogenase (ambiguous), TyrAAT1, TyrAAT2, and TyrAa.

References

• Byng G, Whitaker R, Flick C, Jensen RA (1981). "Enzymology of L-tyrosine biosynthesis in corn (Zea mays)". Phytochemistry. 20 (6): 1289–1292. doi: 10.1016/0031-9422(81)80023-4.
• Gaines CG, Byng GS, Whitaker RJ, Jensen RA (1982). "L-Tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes". Planta. 156 (3): 233–240. doi: 10.1007/BF00393730. PMID  24272471. S2CID  20673627.
• Ishikawa T, Hirayama J, Kobayashi Y, Todo T (2002). "Zebrafish CRY represses transcription mediated by CLOCK-BMAL heterodimer without inhibiting its binding to DNA". Genes Cells. 7 (10): 1073–86. doi: 10.1046/j.1365-2443.2002.00579.x. PMID  12354100.
• Bonner CA, Jensen RA, Gander JE, Keyhani NO (2004). "A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis". Biochem. J. 382 (Pt 1): 279–91. doi: 10.1042/BJ20031809. PMC  1133941. PMID  15171683.