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.
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Received 16 June 2005; received after revision 19 July 2005; accepted 9 August 2005
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Szeltner, Z., Alshafee, I., Juhász, T. et al. The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity. Cell. Mol. Life Sci. 62, 2376–2381 (2005). https://doi.org/10.1007/s00018-005-5262-5
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DOI: https://doi.org/10.1007/s00018-005-5262-5