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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
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1437-4315
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Volume 393, Issue 1-2

Issues

Reactive cysteine in the active-site motif of Bacteroides thetaiotaomicron dipeptidyl peptidase III is a regulatory residue for enzyme activity

Bojana Vukelić
  • Division of Organic Chemistry and Biochemistry, Rudjer Bošković Institute, Bijenička cesta 54, 10002 Zagreb, Croatia
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/ Branka Salopek-Sondi
  • Division of Molecular Biology, Rudjer Bošković Institute, Bijenička cesta 54, 10002 Zagreb, Croatia
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/ Jasminka Špoljarić
  • Division of Organic Chemistry and Biochemistry, Rudjer Bošković Institute, Bijenička cesta 54, 10002 Zagreb, Croatia
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/ Igor Sabljić
  • Division of Physical Chemistry, Rudjer Bošković Institute, Bijenička cesta 54, 10002 Zagreb, Croatia
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/ Nevenka Meštrović
  • Division of Molecular Biology, Rudjer Bošković Institute, Bijenička cesta 54, 10002 Zagreb, Croatia
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/ Dejan Agić
  • Department of Chemistry, Faculty of Agriculture, The Josip Juraj Strossmayer University, Trg Sv. Trojstva 3, 31107 Osijek, Croatia
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/ Marija Abramić
  • Division of Organic Chemistry and Biochemistry, Rudjer Bošković Institute, Bijenička cesta 54, 10002 Zagreb, Croatia
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Published Online: 2012-01-04 | DOI: https://doi.org/10.1515/BC-2011-193

Abstract

Dipeptidyl peptidase III (DPP III), a member of the metallopeptidase family M49, was considered as an exclusively eukaryotic enzyme involved in intracellular peptide cata­bolism and pain modulation. In 2003, new data on genome sequences revealed the first prokaryotic orthologs, which showed low sequence similarity to eukaryotic ones and a cysteine (Cys) residue in the zinc-binding motif HEXXGH. Here we report the cloning and heterologous expression of DPP III from the human gut symbiont Bacteroides thetaiotaomicron. The catalytic efficiency of bacterial DPP III for preferred synthetic substrate hydrolysis was very similar to that of the human host enzyme. Substitution of Cys450 from the active-site motif by serine did not substantially change the enzymatic activity. However, this residue was wholly responsible for the inactivation effect of sulfhydryl reagents. Molecular modeling indicated seven basic amino acid residues in the local environment of Cys450 as a possible cause for its high reactivity. Sequence analysis of 81 bacterial M49 peptidases showed conservation of the HECLGH motif in 68 primary structures with the majority of proteins lacking an active-site Cys originated from aerobic bacteria. Data obtained suggest that Cys450 of B. thetaiotaomicron DPP III is a regulatory residue for the enzyme activity.

This article offers supplementary material which is provided at the end of the article.

Keywords: anaerobic bacteria; enzyme mutation; metallopeptidase M49; sulfhydryl reagent.

About the article

Corresponding author


Received: 2011-07-26

Accepted: 2011-11-17

Published Online: 2012-01-04

Published in Print: 2012-01-01


Citation Information: Biological Chemistry, Volume 393, Issue 1-2, Pages 37–46, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC-2011-193.

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