Jobin_2005_J.Bacteriol_187_795

Reference

Title : Cloning, purification, and enzymatic properties of dipeptidyl peptidase IV from the swine pathogen Streptococcus suis - Jobin_2005_J.Bacteriol_187_795
Author(s) : Jobin MC , Martinez G , Motard J , Gottschalk M , Grenier D
Ref : Journal of Bacteriology , 187 :795 , 2005
Abstract :

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 showed a high affinity for the synthetic peptide glycine-proline-p-nitroanilide and was strongly inhibited by Hg2+ and diprotin A.

PubMedSearch : Jobin_2005_J.Bacteriol_187_795
PubMedID: 15629953
Gene_locus related to this paper: strsu-q673u2

Related information

Gene_locus strsu-q673u2

Citations formats

Jobin MC, Martinez G, Motard J, Gottschalk M, Grenier D (2005)
Cloning, purification, and enzymatic properties of dipeptidyl peptidase IV from the swine pathogen Streptococcus suis
Journal of Bacteriology 187 :795

Jobin MC, Martinez G, Motard J, Gottschalk M, Grenier D (2005)
Journal of Bacteriology 187 :795