title: Proline specific endo- and exopeptidases.
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.
mesh_terms: D000626:Aminopeptidases / Q000378:metabolism; D000804:Angiotensin II / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000201:enzymology; D002268:Carboxypeptidases / Q000378:metabolism; D004150:Dipeptidases / Q000378:metabolism; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D005417:Flavobacterium / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism*; D011392:Proline / Q000378:metabolism*; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases; D013379:Substrate Specificity
chemical_list: D000804:Angiotensin II; D011392:Proline; C025427:carboxypeptidase P; D002268:Carboxypeptidases; D010450:Endopeptidases; D010447:Peptide Hydrolases; D000626:Aminopeptidases; C022450:prolyl aminopeptidase; C022750:X-Pro aminopeptidase; D004150:Dipeptidases; C022454:prolyl dipeptidase; C022449:proline dipeptidase; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C022448:lysosomal Pro-X carboxypeptidase; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases