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Prolyl endopeptidase.

S Wilk
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Abstract

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.

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AnimalsEndopeptidasesHumansPeptidesProlyl OligopeptidasesSerine EndopeptidasesJournal ArticleResearch Support, U.S. Gov't, P.H.S.Review

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BibTeXRIS

S Wilk. 1983-11-28. Prolyl endopeptidase.. https://doi.org/10.1016/0024-3205(83)90285-0

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