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Evaluation of P1' substrate specificity of staphylococcal SplB protease.
- Source :
-
Acta biochimica Polonica [Acta Biochim Pol] 2014; Vol. 61 (1), pp. 149-52. Date of Electronic Publication: 2014 Mar 20. - Publication Year :
- 2014
-
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.
- Subjects :
- Amino Acid Sequence
Humans
Hydrolysis
Kinetics
Staphylococcal Infections genetics
Staphylococcal Infections pathology
Staphylococcus aureus metabolism
Staphylococcus aureus pathogenicity
Substrate Specificity
Bacterial Proteins metabolism
Peptide Hydrolases metabolism
Serine Proteases metabolism
Staphylococcal Infections enzymology
Staphylococcus aureus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1734-154X
- Volume :
- 61
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Acta biochimica Polonica
- Publication Type :
- Academic Journal
- Accession number :
- 24649483