| Literature DB >> 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.Entities:
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Year: 1988 PMID: 3124763 DOI: 10.1016/0003-9861(88)90513-9
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013