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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
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 391, Issue 10

Issues

Amino acid residues modulating the activities of staphylococcal glutamyl endopeptidases

Toshio Ono
  • Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
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/ Yuko Ohara-Nemoto
  • Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
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/ Yu Shimoyama
  • Department of Pathogenesis and Control of Oral Diseases, Division of Oral Microbiology and Immunology, Iwate Medical University School of Dentistry, 1-3-27 Chuodori, Morioka 020-8505, Japan
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/ Hisami Okawara
  • Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
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/ Takeshi Kobayakawa
  • Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
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/ Tomomi T. Baba
  • Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
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/ Shigenobu Kimura
  • Department of Pathogenesis and Control of Oral Diseases, Division of Oral Microbiology and Immunology, Iwate Medical University School of Dentistry, 1-3-27 Chuodori, Morioka 020-8505, Japan
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/ Takayuki K. Nemoto
  • Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
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Published Online: 2010-08-13 | DOI: https://doi.org/10.1515/bc.2010.116

Abstract

The glutamyl endopeptidase family of enzymes from staphylococci has been shown to be important virulence determinants of pathogenic family members, such as Staphylococcus aureus. Previous studies have identified the N-terminus and residues from positions 185–195 as potentially important regions that determine the activity of three members of the family. Cloning and sequencing of the new family members from Staphylococcus caprae (GluScpr) and Staphylococcus cohnii (GluScoh) revealed that the N-terminal Val residue is maintained in all family members. Mutants of the GluV8 enzyme from S. aureus with altered N-terminal residues, including amino acids with similar properties, were inactive, indicating that the Val residue is specifically required at the N-terminus of this enzyme family in order for them to function correctly. Recombinant GluScpr was found to have peptidase activity intermediate between GluV8 and GluSE from Staphylococcus epidermis and to be somewhat less specific in its substrate requirements than other family members. The 185–195 region was found to contribute to the activity of GluScpr, although other regions of the enzyme must also play a role in defining the activity. Our results strongly indicate the importance of the N-terminal and the 185–195 region in the activity of the glutamyl endopeptidases of staphylococci.

Keywords: processing; Staphylococcus aureus; Staphylococcus caprae; Staphylococcus cohnii; Staphylococcus epidermidis; thermolysin

About the article

Corresponding author


Received: 2010-02-07

Accepted: 2010-06-14

Published Online: 2010-08-13

Published in Print: 2010-10-01


Citation Information: Biological Chemistry, Volume 391, Issue 10, Pages 1221–1232, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.116.

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