Arogenate dehydrogenase

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

cyclohexadienyl dehydrogenase
Identifiers
EC no.1.3.1.43
CAS no.64295-75-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
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.