| 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
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. 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.
| 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
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. 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.