Abstract
A bacterial dipeptidyl carboxypeptidase (DCP) released Gly 9-Leu 10-Met 11-NH 2, Leu 10-Met 11-NH 2, Phe 7-Phe 8, and Phe 8-Gly 9 from substance P. HPLC analysis showed that bacterial DCP cleaved substance P at Phe 8-Gly 9, and Gly 9-Leu 10 to release C-terminal tri- and dipeptides (ratio = 14:1). DCP could not release the C-terminal dipeptide from substance P fragments.
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