Mutagenesis in vitro has been used to obtain mutant forms of the bifunctional enzyme, chorismate mutase/ prephenate dehydrogenase. Plasmid DNA containing the genes that code for the enzyme was treated with hydroxylamine and the resulting products were used to transform strains of Eschericliia coli. Two types of mutant were isolated. One contained enzyme which was niutase‐positive, dehydrogenase‐negative while the other not exhibit either activity. Kinetic and physical analysis of one of the purified monofunctional enzymes showed that the loss of dehydrogenase activity was due to modification of the binding site for NAD. The results open the way for molecular studies of structure‐function relationships with this bifunctional enzyme.
|Number of pages||7|
|Journal||European Journal of Biochemistry|
|Publication status||Published - 1 Jan 1982|