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The Nature of the Anthranilic Acid Synthetase Complex of Escherichia coli

From the ¹ From the Department of Biological Sciences, Stanford University, Stanford, California 94305

Nonsense mutants with alterations in the E or D gene of the tryptophan operon lack anthranilate synthetase activity. This activity is detected when extracts of D and E mutants are combined. The interacting component in each mutant extract has a low s value, while the active species in the mixture has a high s value and consists of both components. The s value of the complex is the same as the value obtained with wild-type anthranilate synthetase. One of the interacting components is the enzyme catalyzing the succeeding step in tryptophan biosynthesis.

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