Cloning, Purification, and Enzymatic Properties of Dipeptidyl Peptidase IV from the Swine Pathogen Streptococcus suis

• DOI: 10.1128/jb.187.2.795-799.2005
• Publication Date: 2005-01-03T18:33:17Z
• Authors: Marie-Claude Jobin; Gabriela Martinez; Julie Motard; Marcelo Gottschalk; Daniel Grenier
• Keywords: Streptococcus suis; Cloning (programming); Dipeptidyl peptidase

ABSTRACT In this study, the dipeptidyl peptidase IV (DPP IV) of 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 calculated molecular mass 85 kDa. amino acid sequence contained Gly-X-Ser-X-X-Gly, which is consensus motif flanking active-site serine shared by proteases. recombinant DPP showed high affinity synthetic peptide glycine-proline- p -nitroanilide strongly inhibited Hg 2+ diprotin A.