Evaluation of P1' substrate specificity of staphylococcal SplB protease

• Authors: Katarzyna Pustelny , Natalia Stach , Benedykt Wladyka , Adam Dubin , Grzegorz Dubin
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

serine protease; serine protease-like; SplB; Staphylococcus aureus; substrate specificity

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2014
• Volume: 61
• Issue: 1
• Pages: 149-152

Dates

published

2014

received

2013-10-30

revised

2014-02-19

accepted

2014-02-20

(unknown)

2014-03-20

Contributors

author

Katarzyna Pustelny

• Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland

author

Natalia Stach

• Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland

author

Benedykt Wladyka

• Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland

author

Adam Dubin

• Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland

author

Grzegorz Dubin

• Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland

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