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Indole-3-glycerol Phosphate Synthetase of Escherichia coli, an Enzyme of the Tryptophan Operon

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

The indole-3-glycerol phosphate synthetase of Escherichia coli was purified to apparent homogeneity and was crystallized. The enzyme is a single polypeptide chain of 45,000 molecular weight with 1 NH₂-terminal methionine residue. The amino acid composition of the protein was determined.

The rate of synthesis of this polypeptide chain in E. coli was found to be identical with the rate of synthesis of the polypeptide chains of the tryptophan synthetase and ß₂ subunits.

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				T. Schwarz, K. Uthoff, C. Klinger, H. E. Meyer, P. Bartholmes, and M. Kaufmann Multifunctional Tryptophan-synthesizing Enzyme. THE MOLECULAR WEIGHT OF THE EUGLENA GRACILIS PROTEIN IS UNEXPECTEDLY LOW J. Biol. Chem., April 18, 1997; 272(16): 10616 - 10623. [Abstract] [Full Text] [PDF]