Amino acid sequence of a carboxypeptidase inhibitor from tomato fruit

Abstract

The amino acid sequence of a 37 residue carboxypeptidase inhibitor from tomato fruit has been determined. The amino terminus was shown to be 2-oxopyrrolidine-5-carboxylic acid by digestion of reduced and S-carboxymethylated inhibitor with pyroglutamate aminopeptidase. The remainder of the sequence was assigned by analysis of peptides which had been generated by specific cleavage at the Asp4-Pro5 bond under acid conditions and by treatment with trypsin. The amino acid sequence of this inhibitor is identical with that of an analogous inhibitor from potatoes in 26 positions, and two of the replacements are highly conservative. The identification of the nonconservative replacements has been used to better define regions of the inhibitor which are not believed to contribute significantly to the free energy of association of the enzyme-inhibitor complex.