Arogenate dehydrogenase (NAD(P)+)
| Arogenate dehydrogenase (NAD(P)+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.79 | ||||||||
| CAS no. | 64295-75-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, arogenate dehydrogenase [NAD(P)+] (EC 1.3.1.79) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-arogenic acid (shown as its conjugate base arogenate) and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are L-tyrosine, reduced NADH, and carbon dioxide. Nicotinamide adenine dinucleotide phosphate can be used as an alternative cofactor.[1] [2] [3]
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
[edit ]- ↑ Enzyme 1.3.1.79 at KEGG Pathway Database.
- ↑ 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年1月21日2 . 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.
