Arogenate dehydratase Rabbit Polyclonal Antibody

Arogenate dehydratase (ADT) (EC 4.2.1.91) is an enzyme that catalyzes the chemical reaction. Hence, this enzyme has one substrate, L-arogenate, but 3 products:L-phenylalanine, H2O, and CO2. Certain forms of the protein have the potential to catalyze a second reaction. This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis. The carboxyl and hydroxide groups attached to the 2,5-cyclohexene ring are eliminated from L-arogenate, leaving as carbon dioxide and water. The 2,5-cyclohexene ring becomes a phenyl ring, and L-phenylalanine is formed. Certain forms of ADT have been shown to exhibit some prephenate dehydratase (PDT) activity in addition to the standard ADT activity described above. Known as cyclohexadienyl dehydratases or carbocyclohexadienyl dehydratases, these forms of the enzyme catalyze the same type of reaction (a decarboxylation and a dehydration) on prephenate. The carboxyl and hydroxide groups attached to the 2,5-cyclohexene ring are removed, leaving phenylpyruvate. ADT catalyzes a reaction categorized by two major changes in the structure of the substrate, these being a decarboxylation and a dehydration; the enzyme removes a carboxyl group and a water molecule (respectively). Both potential products of this reaction (L-arogenate and phenylpyruvate) occur at or near the end of the biosynthetic pathway. Total synthesis of L-arogenate has been reported.