Arogenate dehydrogenase
| cyclohexadienyl dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.43 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an arogenate dehydrogenase (EC 1.3.1.43) is an enzyme that catalyzes the chemical reaction
- L-arogenate + NAD+ L-tyrosine + NADH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NAD+, whereas its 3 products are L-tyrosine, NADH, 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+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, pretyrosine dehydrogenase (ambiguous), and L-arogenate:NAD+ oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2F1K.
References
[edit]- Stenmark SL, Pierson DL, Jensen RA, Glover GI (1974). "Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway". Nature. 247 (439): 290–2. Bibcode:1974Natur.247..290S. doi:10.1038/247290a0. PMID 4206476. S2CID 4200115.
- Byng G, Whitaker R, Flick C, Jensen RA (1981). "Enzymology of L-tyrosine biosynthesis in corn (Zea mays)". Phytochemistry. 20 (6): 1289–1292. Bibcode:1981PChem..20.1289B. doi:10.1016/0031-9422(81)80023-4.
- Mayer E, Waldner-Sander S, Keller B, Keller E, Lingens F (1985). "Purification of arogenate dehydrogenase from Phenylobacterium immobile". FEBS Lett. 179 (2): 208–12. Bibcode:1985FEBSL.179..208M. doi:10.1016/0014-5793(85)80519-6. PMID 3967752. S2CID 35594546.
- Lingens F, Keller E, Keller B (1987). "Arogenate dehydrogenase from Phenylobacterium immobile". Metabolism of Aromatic Amino Acids and Amines. Methods in Enzymology. Vol. 142. pp. 513–518. doi:10.1016/S0076-6879(87)42064-8. ISBN 978-0-12-182042-8.
- Zamir LO, Tiberio R, Devor KA, Sauriol F, Ahmad S, Jensen RA (1988). "Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa". J. Biol. Chem. 263 (33): 17284–90. doi:10.1016/S0021-9258(19)77833-8. PMID 2972718.
