Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing.

@article{Nickerson2007ActivationOT,
  title={Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing.},
  author={Nicholas N. Nickerson and L Karthik Prasad and Latha E Jacob and Louis T. J. Delbaere and Martin J. McGavin},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 47},
  pages={34129-38}
}
The serine and cysteine proteases SspA and SspB of Staphylococcus aureus are secreted as inactive zymogens, zSspA and zSspB. Mature SspA is a trypsin-like glutamyl endopeptidase and is required to activate zSspB. Although a metalloprotease Aureolysin (Aur) is in turn thought to contribute to activation of zSspA, a specific role has not been demonstrated. We found that pre-zSspA is processed by signal peptidase at ANA(29) downward arrow, releasing a Leu(30) isoform that is first processed… CONTINUE READING
20 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 20 extracted citations

Similar Papers

Loading similar papers…