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Tryptophan Synthetase ß₂ Subunit

APPLICATION OF GENETIC ANALYSIS TO THE STUDY OF PRIMARY STRUCTURE

From the ¹ From the Department of Microbiology, Scripps Clinic and Research Foundation, La Jolla, California 92037

The amino acid substitution caused by the inactivating point mutation, trpB244, in tryptophan synthetase ß₂ subunit (Escherichia coli K-12) was found to be Lys Asn. This alteration was characterized in the tryptic, chymotryptic, and cyanogen bromide fragments containing the substitution. When the sequence of the 35-residue cyanogen bromide fragment was obtained, this proved to comprise the COOH terminus of the protein.

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				L.-h. Yang, S. A. Ahmed, S. Rhee, and E. W. Miles Importance of Conserved and Variable C-terminal Residues for the Activity and Thermal Stability of the beta Subunit of Tryptophan Synthase J. Biol. Chem., March 21, 1997; 272(12): 7859 - 7866. [Abstract] [Full Text] [PDF]