The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity

Z. Szeltner, I. Alshafee, T. Juhász, R. Parvari, L. Polgár

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The PREPL (previously called KIAA0436) gene encodes a putative serine peptidase from the prolyl oligopeptidase family. A chromosomal deletion involving the PREPL gene leads to a severe syndrome with multiple symptoms. Homology with oligopeptidase B suggested that the enzyme cleaves after an arginine or lysine residue. Several PREPL splice variants have been identified, and a 638-residue variant (PREPL A) was expressed in Escherichia coli and purified. Its secondary structure was similar to that of oligopeptidase B, but differential-scanning calorimetry indicated a higher conformational stability. Dimerization may account for the enhanced stability. Unexpectedly, the PREPL A protein did not cleave peptide substrates containing a P1 basic residue, but did slowly hydrolyse an activated ester substrate, and reacted with diisopropyl fluorophosphate. These results indicated that the catalytic serine is a reactive residue. However, the negligible hydrolytic activity suggests that the function of PREPL A is different from that of the other members of the prolyl oligopeptidase family.

Original languageEnglish
Pages (from-to)2376-2381
Number of pages6
JournalCellular and Molecular Life Sciences
Volume62
Issue number19-20
DOIs
Publication statusPublished - Oct 1 2005

Keywords

  • Denaturation
  • Dimerization
  • Hydrolytic activity
  • KIAA0436
  • Oligopeptidase B
  • Protein expression and isolation

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

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