Cloning, purification, and enzymatic properties of dipeptidyl peptidase IV from the swine pathogen Streptococcus suis.
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.
Jobin
Marie-Claude
MC
Groupe de Recherche en Ecologie Buccale, Faculté de Médecine Dentaire, Université Laval, Quebec City, Quebec, Canada G1K 7P4.
Martinez
Gabriela
G
Motard
Julie
J
Gottschalk
Marcelo
M
Grenier
Daniel
D
D020816:Amino Acid Motifs; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000737:chemistry / Q000302:isolation & purification; D018819:Dipeptidyl Peptidase 4 / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D017669:Mercury Compounds / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000494:pharmacology; D016366:Open Reading Frames; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D017422:Sequence Analysis, DNA; D012697:Serine Endopeptidases / Q000235:genetics; D017011:Streptococcus suis / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
D004269:DNA, Bacterial; D004791:Enzyme Inhibitors; D017669:Mercury Compounds; D009842:Oligopeptides; D011994:Recombinant Proteins; C041445:diprotin A; D018819:Dipeptidyl Peptidase 4; D012697:Serine Endopeptidases