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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

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Band 390, Heft 3

Hefte

Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases

Takayuki K. Nemoto
  • 1Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8588, Japan
  • Weitere Artikel des Autors:
  • De Gruyter OnlineGoogle Scholar
/ Toshio Ono
  • 2Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8588, Japan
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/ Yu Shimoyama
  • 3Department of Oral Microbiology, Iwate Medical University School of Dentistry, Morioka 020-8505, Japan
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/ Shigenobu Kimura
  • 4Department of Oral Microbiology, Iwate Medical University School of Dentistry, Morioka 020-8505, Japan
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  • De Gruyter OnlineGoogle Scholar
/ Yuko Ohara-Nemoto
  • 5Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8588, Japan
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  • De Gruyter OnlineGoogle Scholar
Online erschienen: 17.12.2008 | DOI: https://doi.org/10.1515/BC.2009.027

Abstract

Staphylococcus aureus, Staphylococcus epidermidis, and Staphylococcus warneri secrete glutamyl endopeptidases, designated GluV8, GluSE, and GluSW, respectively. The order of their protease activities is GluSE<GluSW<<GluV8. In the present study, we investigated the mechanism that causes these differences. Expression of chimeric proteins between GluV8 and GluSE revealed that the difference is primarily attributed to amino acid residues 170–195, which define the intrinsic protease activity, and additionally to residues 119–169, which affect the proteolytic sensitivity. Among nine substitutions present in residues 170–195 of the three proteases, the substitutions at positions 185, 188, and 189 were responsible for the changes in their activities, and the combination of W185, V188, and P189, which naturally occurs in GluV8, exerts the highest protease activity. W185 and P189 were indispensable for full activity, but V188 could be replaced by hydrophobic amino acids. These three amino acid residues appear to create a substrate-binding pocket together with the catalytic triad and the N-terminal V1, and therefore define the K m values of the proteases. We also describe a method to produce a chimeric form of GluSE and GluV8 that is resistant to proteolysis, and therefore possesses 4-fold higher activity than the wild-type recombinant GluV8.

Keywords: glutamyl endopeptidase; Staphylococcus aureus; Staphylococcus epidermidis; substrate-binding pocket; V8 protease

Artikelinformationen

Corresponding author


Erhalten: 13.10.2008

Angenommen: 29.11.2008

Online erschienen: 17.12.2008

Erschienen im Druck: 01.03.2009


Quellenangabe: Biological Chemistry, Band 390, Heft 3, Seiten 277–285, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.027.

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