释义 |
- Structural studies
- References
{{enzyme | Name = cyclohexadienyl dehydrogenase | EC_number = 1.3.1.43 | CAS_number = 64295-75-6 | IUBMB_EC_number = 1/3/1/43 | GO_code = 0047794 | image = | width = | caption = }}In enzymology, an arogenate dehydrogenase ({{EC number|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 studiesAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code {{PDB link|2F1K}}. References- {{cite journal | vauthors = Stenmark SL, Pierson DL, Jensen RA, Glover GI | date = 1974 | title = Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway | journal = Nature | volume = 247 | pages = 290–2 | pmid = 4206476 | doi = 10.1038/247290a0 | issue = 439 }}
- {{cite journal | vauthors = Byng G, Whitaker R, Flick C, Jensen RA | last-author-amp = yes | date = 1981 | title = Enzymology of L-tyrosine biosynthesis in corn (Zea mays) | journal = Phytochemistry | volume = 20 | pages = 1289–1292 | doi = 10.1016/0031-9422(81)80023-4 | issue = 6 }}
- {{cite journal | vauthors = Mayer E, Waldner-Sander S, Keller B, Keller E, Lingens F | date = 1985 | title = Purification of arogenate dehydrogenase from Phenylobacterium immobile | journal = FEBS Lett. | volume = 179 | pages = 208–12 | pmid = 3967752 | doi = 10.1016/0014-5793(85)80519-6 | issue = 2 }}
- {{cite journal | vauthors = Lingens F, Keller E, Keller B | last-author-amp = yes | date = 1987 | title = Arogenate dehydrogenase from Phenylobacterium immobile | journal = Methods Enzymol. | volume = 142 | pages = 513–518 | doi = 10.1016/S0076-6879(87)42064-8 | series = Methods in Enzymology | isbn = 978-0-12-182042-8 }}
- {{cite journal | vauthors = Zamir LO, Tiberio R, Devor KA, Sauriol F, Ahmad S, Jensen RA | date = 1988 | title = Structure of D-prephenyllactate. A carboxycyclohexadienyl metabolite from Neurospora crassa | journal = J. Biol. Chem. | volume = 263 | pages = 17284–90 | pmid = 2972718 | issue = 33 }}
{{CH-CH oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.3-enzyme-stub}} 3 : EC 1.3.1|NADH-dependent enzymes|Enzymes of known structure |