Prolyl endopeptidase.
Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. The structure of beta-neo-endorphin suggests that this opioid peptide is formed by the action of prolyl endopeptidase on a precursor of higher molecular weight. Formation of two biologically active fragments of substance P also requires the action of this enzyme. This review summarizes the current knowledge of the biochemistry of this enzyme, and its potential significance for neuropeptide physiology and pharmacology.
D000818:Animals; D010450:Endopeptidases / Q000032:analysis / Q000302:isolation & purification / Q000502:physiology*; D006801:Humans; D010455:Peptides / Q000378:metabolism; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases
D010455:Peptides; D010450:Endopeptidases; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases