Proline specific peptidases

• Published in: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology 1997-12, Vol.1343 (2), p.160-186
• Main Authors: Cunningham, Damian F, O'Connor, Brendan
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Aminopeptidase P; Animals; Dipeptidyl peptidase IV and II; Endopeptidases - chemistry; Endopeptidases - metabolism; Endopeptidases - physiology; Enzyme Inhibitors - pharmacology; Humans; Molecular Sequence Data; Molecular Structure; Peptides - chemistry; Peptides - metabolism; Prolidase; Prolinase; Proline; Proline - chemistry; Proline - metabolism; Prolyl oligopeptidase; Substrate Specificity
• ISSN: 0167-4838; 0006-3002; 1879-2588
• DOI: 10.1016/S0167-4838(97)00134-9

Proline is unique among the 20 amino acids due to its cyclic structure. This specific conformation imposes many restrictions on the structural aspects of peptides and proteins and confers particular biological properties upon a wide range of physiologically important biomolecules. In order to adequately deal with such peptides, nature has developed a group of enzymes that recognise this residue specifically. These peptidases cover practically all situations where a proline residue might occur in a potential substrate. In this paper we endeavour to discuss these enzymes, particularly those responsible for peptide or protein hydrolysis at proline sites. We have detailed their discovery, biochemical attributes and substrate specificities and have provided information as to the methodology used to detect and manipulate their activities. We have also described the roles, or potential roles that these enzymes may play physiologically and the consequences of their dysfunction in varied disease states.