A processing enzyme for prodynorphin derived peptides.
Copyright policy )A processing enzyme for prodynorphin derived peptides.
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.
Cysteine Endopeptidases, Kinetics, Metalloendopeptidases, Amino Acid Sequence, Enkephalins, Protein Precursors, Protein Processing, Post-Translational, Substrate Specificity
Cysteine Endopeptidases, Kinetics, Metalloendopeptidases, Amino Acid Sequence, Enkephalins, Protein Precursors, Protein Processing, Post-Translational, Substrate Specificity
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