A processing enzyme for prodynorphin derived peptides

NIDA Res Monogr. 1986:75:247-50.

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

  • Amino Acid Sequence
  • Cysteine Endopeptidases / metabolism*
  • Enkephalins / genetics*
  • Kinetics
  • Metalloendopeptidases*
  • Protein Precursors / genetics*
  • Protein Processing, Post-Translational*
  • Substrate Specificity

Substances

  • Enkephalins
  • Protein Precursors
  • preproenkephalin
  • Cysteine Endopeptidases
  • Metalloendopeptidases
  • thimet oligopeptidase