Arogenate dehydratase
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In enzymology, an arogenate dehydratase (EC 4.2.1.91) is an enzyme that catalyzes the chemical reaction
- L-arogenate L-phenylalanine + H2O + CO2
Hence, this enzyme has one substrate, L-arogenate, but 3 products: L-phenylalanine, H2O, and CO2.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming). Other names in common use include carboxycyclohexadienyl dehydratase, and L-arogenate hydro-lyase (decarboxylating). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
[edit] References
- IUBMB entry for 4.2.1.91
- BRENDA references for 4.2.1.91 (Recommended.)
- PubMed references for 4.2.1.91
- PubMed Central references for 4.2.1.91
- Google Scholar references for 4.2.1.91
- Fischer R, Jensen R (1987). "Arogenate dehydratase". Methods. Enzymol. 142: 495–502. PMID 3600377.
- 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: 17284–90. PMID 2972718.
- Siehl DL, Conn EE (1988). "Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench". Arch. Biochem. Biophys. 260: 822–9. PMID 3124763.