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A processing enzyme for prodynorphin derived peptides
K M Metters1, J Rossier, E E Oliveira
1Laboratoire de Physiologie Nerveuse, C.N.R.S., Gif-sur-Yvette, France.
NIDA Research Monograph
|January 1, 1986
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.