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In enzymology, an arogenate dehydrogenase (NADP+) (EC 1.3.1.78) is an enzyme that catalyzes the chemical reaction
| arogenate dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.78 | ||||||||
| CAS no. | 64295-75-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- L-arogenate + NADP+ 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
edit- 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.
