Amino acid residues modulating the activities of staphylococcal glutamyl endopeptidases
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Toshio Ono
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.
©2010 by Walter de Gruyter Berlin New York
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- Guest Editorial
- Highlight: The Biology of Aging: Mechanisms and Intervention
- Highlight: 61th Mosbach Colloquium of the GBM ‘The Biology of Aging: Mechanisms and Intervention’
- Multiplex analysis of mitochondrial DNA pathogenic and polymorphic sequence variants
- The hypoxia-inducible factor HIF-1 functions as both a positive and negative modulator of aging
- E. coli hypoxia-inducible factor ArcA mediates lifespan extension in a lipoic acid synthase mutant by suppressing acetyl-CoA synthetase
- Glucose homeostasis and insulin sensitivity in growth hormone-transgenic mice: a cross-sectional analysis
- PROTEIN STRUCTURE AND FUNCTION
- New structural aspects of FKBP38 activation
- The neuronal proteins CIPP, Cypin and IRSp53 form a tripartite complex mediated by PDZ and SH3 domains
- CELL BIOLOGY AND SIGNALING
- Inhibition of interferon-α-induced signaling by hyperosmolarity and hydrophobic bile acids
- Role of the second disulfide bridge (Cys18-Cys274) in stabilizing the inactive AT1 receptor
- Demonstration of protein absorption in the intestinal epithelium of fish and mice by laser scanning confocal microscopy
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- Amino acid residues modulating the activities of staphylococcal glutamyl endopeptidases
