Proline specific endo- and exopeptidases
- 1 April 1980
- journal article
- review article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 30 (2) , 111-127
- https://doi.org/10.1007/bf00227927
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 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.Keywords
This publication has 90 references indexed in Scilit:
- SIZE AND SHAPE OF TWO INTESTINAL DIPEPTIDASESInternational Journal of Peptide and Protein Research, 2009
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Liver dipeptidyl aminopeptidase IV hydrolyzes substance PFEBS Letters, 1978
- Serum glycylproline p-nitroanilidase activity in human hypertensionClinica Chimica Acta; International Journal of Clinical Chemistry, 1977
- Proline endopeptidase and exopeptidase activity in polymorphonuclear granulocytesMolecular and Cellular Biochemistry, 1976
- Enzymatic Properties of Pig Intestinal Proline Dipeptidase.Acta Chemica Scandinavica, 1974
- Separation and Characterization of Three Proline Peptidases from a Strain of Arthrobacter.Acta Chemica Scandinavica, 1971
- The Cleavage of Prolyl Peptides by Kidney PeptidasesEuropean Journal of Biochemistry, 1970
- Brain aminoacyl arylamidase. Further purification of the soluble bovine enzyme and studies on substrate specificity and possible active-site residuesBiochemistry, 1970
- Aminopeptidase-PBiochemical and Biophysical Research Communications, 1968