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Title: Proline specific endo- and exopeptidases. Author: Walter R, Simmons WH, Yoshimoto T. Journal: Mol Cell Biochem; 1980 Apr 18; 30(2):111-27. PubMed ID: 6991912. Abstract: Peptidases which are specific for proline residues have been described and include endopeptidases (post-proline cleaving enzyme and proline specific endopeptidase), N-terminal exopeptidases (post-proline dipeptidyl aminopeptidase, proline iminopeptidase, aminopeptidase P), C-terminal exopeptidases (prolylcarboxypeptidase, and carboxypeptidase P) and dipeptidases (prolyl dipeptidase and proline dipeptidase). The properties, distinguishing charcteristics, and possible significance of these proline specific endo- and exopeptidases are discussed. In addition, reference is made to a series of enzymes which can hydrolyze proline containing peptide bonds, but which are not specific for proline.[Abstract] [Full Text] [Related] [New Search]