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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 391, Issue 12

Issues

Kinetic and structural characterization of bacterial glutaminyl cyclases from Zymomonas mobilis and Myxococcus xanthus

David Ruiz Carrillo
  • Probiodrug AG, Weinbergweg 22, D-06120 Halle/Saale, Germany
  • Institut für Biochemie und Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Straße 3, D-06120 Halle/Saale, Germany
  • These authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Christoph Parthier
  • Institut für Biochemie und Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Straße 3, D-06120 Halle/Saale, Germany
  • These authors contributed equally to this work.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Nadine Jänckel / Julia Grandke / Marco Stelter
  • Probiodrug AG, Weinbergweg 22, D-06120 Halle/Saale, Germany
  • Institut für Biochemie und Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Straße 3, D-06120 Halle/Saale, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Stephan Schilling / Mathias Boehme / Piotr Neumann
  • Institut für Biochemie und Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Straße 3, D-06120 Halle/Saale, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Raik Wolf / Hans-Ulrich Demuth / Milton T. Stubbs
  • Institut für Biochemie und Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Straße 3, D-06120 Halle/Saale, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jens-Ulrich Rahfeld
Published Online: 2010-09-24 | DOI: https://doi.org/10.1515/bc.2010.130

Abstract

Although enzymes responsible for the cyclization of amino-terminal glutamine residues are present in both plant and mammal species, none have yet been characterized in bacteria. Based on low sequence homologies to plant glutaminyl cyclases (QCs), we cloned the coding sequences of putative microbial QCs from Zymomonas mobilis (ZmQC) and Myxococcus xanthus (MxQC). The two recombinant enzymes exhibited distinct QC activity, with specificity constants k cat /K m of 1.47±0.33 mm -1 s-1 (ZmQC) and 142±32.7 mm -1 s-1 (MxQC) towards the fluorescent substrate glutamine-7-amino-4-methyl-coumarine. The measured pH-rate profile of the second order rate constant displayed an interesting deviation towards the acidic limb of the pH chart in the case of ZmQC, whereas MxQC showed maximum activity in the mild alkaline pH range. Analysis of the enzyme variants ZmQCGlu46Gln and MxQCGln46Glu show that the exchanged residues play a significant role in the pH behaviour of the respective enzymes. In addition, we determined the three dimensional crystal structures of both enzymes. The tertiary structure is defined by a five-bladed β-propeller anchored by a core cation. The structures corroborate the putative location of the active site and confirm the proposed relation between bacterial and plant glutaminyl cyclases.

Keywords: bacterial; glutaminyl cyclase; microbial; pH-rate dependency; pyroglutamate; QC

About the article

Corresponding authors ;


Received: 2010-06-30

Accepted: 2010-08-05

Published Online: 2010-09-24

Published in Print: 2010-12-01


Citation Information: Biological Chemistry, Volume 391, Issue 12, Pages 1419–1428, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.130.

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