Arogenate dehydrogenase

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
cyclohexadienyl dehydrogenase
Identifiers
EC number1.3.1.43
CAS number64295-75-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

gollark: Like I said, it's iterative and not recursive now, so no call stack issues.
gollark: If this ever becomes a "serious" esolang, our interpreter will be COOLER™ than its competitors in some ways.
gollark: Well, yes, I'm not going to, but it's neat.
gollark: Although the spec limits the maximum recursion depth anyway.
gollark: So you can execute [ESOLANG REDACTED] without fear of stack overflows.

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. doi:10.1038/247290a0. PMID 4206476.
    • 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.
    • 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.


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