Abstract
The pattern of induction and regulatory properties of the enzymes chorismate mutase, prephenate dehydratase, and anthranilate synthetase were investigated in a chloramphenicol-producing Streptomycete under a variety of environmental conditions. The enzymes were not subject to repression by intermediates or end products of the shikimic acid pathway. Throughout purification procedures chorismate mutase and prephenate dehydratase activities were each represented by single enzyme proteins of molecular weights 75 000 and 220 000, respectively. Chorismate mutase activity was not inhibited by end products or intermediates of the shikimic acid pathway. Prephenate dehydratase activity was controlled solely by feedback inhibition by L-phenylalanine, and anthranilate synthetase activity was only inhibited by L-tryptophan.
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