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J Biol Chem, Vol. 274, Issue 14, 9246-9252, April 2, 1999

Prolyl Tripeptidyl Peptidase from Porphyromonas gingivalis
A NOVEL ENZYME WITH POSSIBLE PATHOLOGICAL IMPLICATIONS FOR THE DEVELOPMENT OF PERIODONTITIS

Agnieszka Banbula, Pawel Mak, Marcin Bugno, Jerzy Silberring^§, Adam Dubin, Daniel Nelson^¶, James Travis^¶, and Jan Potempa^¶

From the  Institute of Molecular Biology and ^§ Faculty of Chemistry and Regional Laboratory, Jagiellonian University, 31-120 Kraków, Poland and the ^¶ Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602

Porphyromonas gingivalis possesses a complex proteolytic system, which is essential for both its growth and evasion of host defense mechanisms. In this report we characterized, both at a protein and genomic level, a novel peptidase of this system with prolyl tripeptidyl peptidase activity. The enzyme was purified to homogeneity, and its enzymatic activity and biochemical properties were investigated. The amino acid sequence at the amino terminus and of internal peptide fragments enabled identification of the gene encoding this enzyme, which we refer to as PtpA for prolyl tripeptidyl peptidase A. The gene encodes an 82-kDa protein, which contains a GWSYGG motif, characteristic for members of the S9 prolyl oligopeptidase family of serine proteases. However, it does not share any structural similarity to other tripeptidyl peptidases, which belong to the subtilisin family. The production of prolyl tripeptidyl peptidase may contribute to the pathogenesis of periodontal tissue destruction through the mutual interaction of this enzyme, host and bacterial collagenases, and dipeptidyl peptidases in the degradation of collagen during the course of infection.

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