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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Cloning, Molecular
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DNA, Bacterial / chemistry
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DNA, Bacterial / isolation & purification
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Dipeptidyl Peptidase 4 / genetics*
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Dipeptidyl Peptidase 4 / isolation & purification
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Dipeptidyl Peptidase 4 / metabolism*
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Enzyme Inhibitors / pharmacology
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Mercury Compounds / pharmacology
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Molecular Sequence Data
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Molecular Weight
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Oligopeptides / pharmacology
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Open Reading Frames
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Analysis, DNA
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Serine Endopeptidases / genetics
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Streptococcus suis / enzymology*
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Streptococcus suis / genetics
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Substrate Specificity
Substances
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DNA, Bacterial
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Enzyme Inhibitors
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Mercury Compounds
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Oligopeptides
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Recombinant Proteins
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diprotin A
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Dipeptidyl Peptidase 4
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Serine Endopeptidases