title: Evaluation of P1' substrate specificity of staphylococcal SplB protease.
abstract: Staphylococcus aureus is a dangerous human pathogen characterized by growing antibiotic resistance. Virulence of S. aureus relies on a variety of secreted and cell surface associated virulence factors among which certain proteolytic enzymes play an important role. Amid staphylococcal extracellular proteases, those encoded by the spl operon remain poorly characterized, both in terms of enzymology and their physiological role. Initial data demonstrated that Spl proteases exhibit restricted substrate specificity. This study describes development of convenient protein FRET substrates for SplB protease and characterization of the substrate preference of the protease at the P1' position. Kinetic data on hydrolysis of a panel of substrates substituted at the said position is provided.
authors.affiliation: Department of Analytical Biochemistry and Department of Cell Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland.
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Pustelny
authors.affiliation: Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland.
authors.forename: Natalia
authors.initials: N
authors.lastname: Stach
authors.affiliation: Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Polandi and Malopolska Centre of Biotechnology, Kraków, Poland.
authors.forename: Benedykt
authors.initials: B
authors.lastname: Wladyka
authors.affiliation: Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland.
authors.forename: Adam
authors.initials: A
authors.lastname: Dubin
authors.affiliation: Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Polan and Malopolska Centre of Biotechnology, Kraków, Poland.
authors.forename: Grzegorz
authors.initials: G
authors.lastname: Dubin
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D010447:Peptide Hydrolases / Q000378:metabolism*; D057057:Serine Proteases / Q000378:metabolism*; D013203:Staphylococcal Infections / Q000201:enzymology* / Q000235:genetics / Q000473:pathology; D013211:Staphylococcus aureus / Q000201:enzymology* / Q000378:metabolism / Q000472:pathogenicity; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D010447:Peptide Hydrolases; D057057:Serine Proteases