title: A processing enzyme for prodynorphin derived peptides.
abstract: Endo-oligopeptidase A known to hydrolyse the Phe5-Ser6 bond of bradykinin and the Arg8-Arg9 bond of neurotensin has been shown to produce, by a single cleavage, leucine5-enkephalin from small prodynorphin derived enkephalin-containing peptides. The specificity constants (kcat/km) obtained for the hydrolysis of bradykinin, neurotensin and dynorphin B are of the same order, suggesting that the substrate amino acid sequence is not the only factor determining the cleavage site of this enzyme.
mesh_terms: D000595:Amino Acid Sequence; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004745:Enkephalins / Q000235:genetics*; D007700:Kinetics; D008666:Metalloendopeptidases; D011498:Protein Precursors / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D013379:Substrate Specificity
chemical_list: D004745:Enkephalins; D011498:Protein Precursors; C033660:preproenkephalin; D003546:Cysteine Endopeptidases; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase