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• W2082464607 abstract "Endo-oligopeptidase A, highly purified from the cytosol fraction of bovine brain by immunoaffinity chromatography, has been characterised as a thiol endopeptidase. This enzyme, 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. [Leu]enkephalin or [Met]enkephalin from small enkephalin-containing peptides. Enkephalin formation could be inhibited in a concentration dependent manner by the alternative substrate bradykinin. The optimal substrate size was found to be 8–13 amino acids, with enkephalin the only product released from precursors in which this sequence is immediately followed by a pair of basic residues. However, the specificity constants (kcat/Km) obtained for endo-oligopeptidase A hydrolysis, neurotensin and dynorphin B are of the same order. Taken together, these results indicate that the substrate amino acid sequence is not the only factor determining the cleavage site of this enzyme. Finally, endo-oligopeptidase A and metalloendopeptidase EC 3.4.24.15 are two different enzymes. The latter is not able to liberate enkephalins from metorphamide and dynorphin1–8." @default.
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• W2082464607 date "1988-01-01" @default.
• W2082464607 modified "2023-09-25" @default.
• W2082464607 title "Liberation of enkephalins from enkephalin-containing peptides by brain endo-oligopeptidase A" @default.
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• W2082464607 doi "https://doi.org/10.1016/0300-9084(88)90157-5" @default.
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