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
Search PMC articles PubMed articles NCBI proteins

In enzymology, an arogenate dehydrogenase (EC 1.3.1.43) is an enzyme that catalyzes the chemical reaction

L-arogenate + NAD⁺${\displaystyle \rightleftharpoons }$ 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

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2F1K.

References

• 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. 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. doi: 10.1016/0014-5793(85)80519-6 . PMID   3967752. S2CID   35594546.
• Lingens F, Keller E, Keller B (1987). "Arogenate dehydrogenase from Phenylobacterium immobile". Methods Enzymol. Methods in Enzymology. 142: 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. PMID   2972718.