Abstract
The amino acid sequences of 28 soluble tryptic peptides from chorismate mutase/prephenate dehydratase from Escherichia coli K12 have been determined. Together with the four unique cysteine-containing peptides sequenced by Gething and Davidson ((1976) Eur. J. Biochem. 71, 327–336) this accounts for approximately 75% of the total sequence expected for this protein. A high frequency of identity between some of the peptides suggests the possibility of gene duplication during the evolution of the structural gene for the enzyme.
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