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

  • David Ruiz Carrillo , Christoph Parthier , Nadine Jänckel , Julia Grandke , Marco Stelter , Stephan Schilling , Mathias Boehme , Piotr Neumann , Raik Wolf , Hans-Ulrich Demuth , Milton T. Stubbs and Jens-Ulrich Rahfeld
Published/Copyright: September 24, 2010
Biological Chemistry
From the journal Volume 391 Issue 12

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 kcat/Km 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
Corresponding authors ;
Received: 2010-6-30
Accepted: 2010-8-5
Published Online: 2010-09-24
Published in Print: 2010-12-01

©2010 by Walter de Gruyter Berlin New York

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  21. Acknowledgement
https://doi.org/10.1515/bc.2010.130
Keywords for this article
bacterial; glutaminyl cyclase; microbial; pH-rate dependency; pyroglutamate; QC

Articles in the same Issue

  1. Minireview
  2. Physiology and pathophysiology of the RANKL/RANK system
  3. Genes and Nucleic Acids
  4. Murine aldo-keto reductase family 1 subfamily B: identification of AKR1B8 as an ortholog of human AKR1B10
  5. Characterization of plant miRNAs and small RNAs derived from potato spindle tuber viroid (PSTVd) in infected tomato
  6. Protein Structure and Function
  7. Characterization of a mutant R11H αB-crystallin associated with human inherited cataract
  8. Secretion of hepatoma-derived growth factor is regulated by N-terminal processing
  9. Twin arginine translocation (Tat)-dependent protein transport: the passenger protein participates in the initial membrane binding step
  10. Kinetic and structural characterization of bacterial glutaminyl cyclases from Zymomonas mobilis and Myxococcus xanthus
  11. Membranes, Lipids, Glycobiology
  12. Quantitative determination of haptoglobin glycoform variants in psoriasis
  13. Molecular Medicine
  14. Bile acid retention and activation of endogenous hepatic farnesoid-X-receptor in the pathogenesis of fatty liver disease in ob/ob-mice
  15. Cell Biology and Signaling
  16. Acute and long-term effects of metformin on the function and insulin secretory responsiveness of clonal β-cells
  17. Proteolysis
  18. Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition
  19. Pharmacological and genetic evidence that cathepsin B is not the physiological activator of rodent prorenin
  20. Acknowledgement
  21. Acknowledgement
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