Cloning, purification, and enzymatic properties of dipeptidyl peptidase IV from the swine pathogen Streptococcus suis.

@article{Jobin2005CloningPA,
  title={Cloning, purification, and enzymatic properties of dipeptidyl peptidase IV from the swine pathogen Streptococcus suis.},
  author={M. E. Jobin and Gabriela Mart{\'i}nez and Julie Motard and Marcelo Gottschalk and Daniel Grenier},
  journal={Journal of bacteriology},
  year={2005},
  volume={187 2},
  pages={795-9}
}
In this study, the dipeptidyl peptidase IV (DPP IV) of the swine pathogen Streptococcus suis was cloned, overexpressed in Escherichia coli, and characterized. The coding region comprises 2,268 nucleotides containing an open reading frame that codes for a 755-amino-acid protein with a calculated molecular mass of 85 kDa. The amino acid sequence contained the sequence Gly-X-Ser-X-X-Gly, which is a consensus motif flanking the active-site serine shared by serine proteases. The recombinant DPP IV… CONTINUE READING