A processing enzyme for prodynorphin derived peptides.

K M Metters; J Rossier; E E Oliveira; O Toffoletto; A C Camargo

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PubMed · 3123940

A processing enzyme for prodynorphin derived peptides.

K M Metters·J Rossier·E E Oliveira·O Toffoletto·A C Camargo

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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.

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Amino Acid Sequence Cysteine Endopeptidases Enkephalins Kinetics Metalloendopeptidases Protein Precursors Protein Processing, Post-Translational Substrate Specificity Journal Article

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K M Metters, J Rossier, E E Oliveira, O Toffoletto, A C Camargo. 1986. A processing enzyme for prodynorphin derived peptides.. https://pubmed.ncbi.nlm.nih.gov/3123940/

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