Endopeptidase 24.16B. A new variant of endopeptidase 24.16

D. Rodd, L. B. Hersh

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

A peptidase, isolated from rat testes, is inhibited by 1 mM o- phenanthroline, 1 μM N-(1-(R,S)-carboxyl-3-phenyl-propyl)-Ala-Ala-Phe-p- aminobenzoate, and 6 mM Pro-Ile, properties similar to those ascribed to endopeptidase 24.16. The enzyme hydrolyzes dynorphin A-8, neurotensin 1-13, angiotensin I, and substance P. Kinetic analysis of a series of angiotensin I analogs showed that substitutions at P-1, P-1', or P-2' had little effect on K(m) or K(cat). Variation of peptide size with a series of dynorphin A peptides showed chain length to be significant. The peptidase cleaved dynorphin A-8 at both Leu5-Arg6 and Arg6-Arg7, and neurotensin 1-13 at Pro10-Tyr11 and Arg8-Arg9. In contrast, rat endopeptidase 24.16 cleaves dynorphin A-8 at Gly4-Leu5 and Leu5-Arg6, and neurotensin 1-13 only at Pro10-Tyr11. These findings, as well as the observation that endopeptidase 24.16 exhibits a considerably higher affinity for Pro-Ile, K(i) = 90 μM, indicates the peptidase isolated in this study is related to, but distinct from, rat endopeptidase 24.16. We propose that this new endopeptidase be referred to as endopeptidase 24.16B, while the originally described enzyme be referred to as endopeptidase 24.16A

Original languageEnglish
Pages (from-to)10056-10061
Number of pages6
JournalJournal of Biological Chemistry
Volume270
Issue number17
DOIs
StatePublished - 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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