Abstract
Summary Porcine pepsin and penicillopepsin catalyze transpeptidation reactions which involve the transfer in high yield of N-terminal leucine from Leu-Tyr-Leu, and Leu-Tyr amide to intact substrate with the subsequent release of Leu-Leu. With the latter substrate porcine pepsin also forms Leu-Leu-Leu. With penicillopepsin small amounts of Leu-Leu-Tyr-Leu and Leu-Leu-Tyr amide resp. were obtained as intermediates from Leu-Tyr-Leu and Leu-Tyr amide. No radioactivity was incorporated into Leu-Leu when Leu-Tyr-Leu and [14C]-leucine (1:6) were incubated with the enzymes. It was concluded that the transpeptidation proceeds via covalent acyl intermediate.
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