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Licensed Unlicensed Requires Authentication Published by De Gruyter January 28, 2013

Hydrolysis of dipeptide derivatives reveals the diversity in the M49 family

  • Nina Jajčanin-Jozić and Marija Abramić EMAIL logo
From the journal Biological Chemistry


Dipeptidyl peptidase III, a metallopeptidase of the M49 family, was first identified (in the pituitary) by its specific cleavage of diarginyl arylamides, which have been used as preferred assay substrates until now. Here we examined the activity of the yeast and human dipeptidyl peptidase III in parallel. The human enzyme preferred Arg2-β-naphthylamide and showed 620-fold higher kcat/Km for this substrate. In contrast, the yeast enzyme did not display a preference for any of the X-Arg-β-naphthylamide analyzed. The replacement of Gly505 with Asp, resulted in a less active, but more selective, yeast enzyme form. These results indicate diversity in cleavage specificity in the M49 family.

Corresponding author: Marija Abramić, Division of Organic Chemistry and Biochemistry, Ruđer Bošković Institute, Bijenička cesta 54, 10002 Zagreb, Croatia

Support for this study by the Croatian Ministry of Science, Education and Sport (Project 098-1191344-2938) is gratefully acknowledged.


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Received: 2012-12-6
Accepted: 2013-1-14
Published Online: 2013-01-28
Published in Print: 2013-06-01

©2013 by Walter de Gruyter Berlin Boston

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