Abstract
The tryptophan synthase beta 2 protein (EC 4.2.1.20) of Escherichia coli, Enterobacter aerogenes, Serratia marcescens, and Erwinia carotovora was purified and compared. Two-dimensional total peptide patterns for each of the four beta2 proteins obtained after digestion with trypsin showed that approximately three quarters of the total peptides are common to all four peptides. Examination of only arginine-containing peptides showed that approximately half of these peptides are common. From a comparative standpoint, the data provide evidence that the primary structure of beta 2 proteins is relatively similar, indicating that the trpB cistron is evolutionarily conserved in the enteric bacteria group.
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