Proline specific endo- and exopeptidases |
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Authors: | Roderich Walter William H Simmons Tadashi Yoshimoto |
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Institution: | (1) Department of Physiology and Biophysics, University of Illinois at the Medical Center, 60612 Chicago, Illinois, U.S.A;(2) Faculty of Pharmaceutical Sciences, Nagasaki University, Bunkyo-machi, 1-14, 852 Nagasaki, Japan |
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Abstract: | Summary 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 characteristics, 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. |
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