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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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PREPL: a putative novel oligopeptidase propelled into the limelight

Kevin Martens1 / Rita Derua2 / Sandra Meulemans3 / Etienne Waelkens4 / Jaak Jaeken5 / Gert Matthijs6 / John W.M. Creemers7

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Corresponding author

Citation Information: Biological Chemistry. Volume 387, Issue 7, Pages 879–883, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2006.111, July 2006

Publication History

Published Online:
2006-07-20

Abstract

The prolyl endopeptidase-like protein PREPL has recently attracted attention because its gene is located within two contiguous gene-deletion syndromes, the 2p21 deletion syndrome and the hypotonia-cystinuria syndrome. Deletion of the gene results in hypotonia at birth, failure to thrive and growth hormone deficiency. PREPL is highly reactive against an activity-based probe, which indicates the presence of an intact catalytic machinery. However, no substrate has been found yet. The unique carboxy-terminus of the catalytic domain might contain the key to the as yet elusive specificity.

Keywords: activity-based probe; enzyme; FP-biotin; hypotonia-cystinuria syndrome; 2p21 deletion syndrome

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