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  • Title: Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench.
    Author: Siehl DL, Conn EE.
    Journal: Arch Biochem Biophys; 1988 Feb 01; 260(2):822-9. PubMed ID: 3124763.
    Abstract:
    Arogenate dehydratase was purified sixfold from an extract of etiolated seedlings of Sorghum bicolor. Prephenate dehydratase was not detected. The arogenate dehydratase activity displayed hyperbolic substrate kinetics with a KM for arogenate of 0.32 mM. Activity was inhibited competitively by phenylalanine and was stimulated by tyrosine. The low KI for phenylalanine (24 microM) and KA for tyrosine (2.5 microM) indicated a high affinity of the enzyme for these effectors. These results establish the routing of metabolites in phenylalanine biosynthesis in sorghum as proceeding via arogenate rather than phenylpyruvate.
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