Arogenate dehydrogenase (NADP+)

From Wikipedia, the free encyclopedia

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

L-arogenate + NADP⁺ $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 1.3.1.78
BRENDA references for 1.3.1.78 (Recommended.)
PubMed references for 1.3.1.78
PubMed Central references for 1.3.1.78
Google Scholar references for 1.3.1.78
Byng G, Whitaker R, Flick C and Jensen RA (1981). "Enzymology of L-tyrosine biosynthesis in corn (Zea mays)". Phytochemistry 20: 1289–1292. doi:10.1016/0031-9422(81)80023-4.
Gaines CG, Byng GS, Whitaker RJ and Jensen RA (1982). "L-Tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes". Planta 156: 233–240. doi:10.1007/BF00393730.
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: 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: 279–91. doi:10.1042/BJ20031809. PMID 15171683.