Prolyl Tripeptidyl Peptidase from Porphyromonas gingivalis

Abstract

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.

Purification and Characterization of a Novel Cysteine Proteinase (Periodontain) from Porphyromonas gingivalis

“…Second, in combination with HNE, periodontain may augment the degradation of peptides produced by the actions of the gingipains. Third, there is evidence that P. gingivalis produces a prolyl dipeptidyl peptidase (49), a prolyl tripeptidyl peptidase (50), and an uncharacterized collagenase. 2 This proteolytic milieu in the GCF could aid in the final production of peptides capable of being taken up by P. gingivalis.…”

Asp- and Glu-specific Novel Dipeptidyl Peptidase 11 of Porphyromonas gingivalis Ensures Utilization of Proteinaceous Energy Sources

“…First, the predominant proteolytic activities of Kgp and Rgps (22)(23)(24)(25) are believed to digest nutritional proteins into oligopeptides. Subsequently, oligopeptides are processed by dipeptidyl peptidase IV (EC 3.4.14.5, DPPIV) (26), DPP7 (27) and prolyl tripeptidyl peptidase-A (PTP-A) (28,29). P. gingivalis DPPIV preferentially cleaves NH 2 -XP2X n and less potently NH 2 -XA2X n (26,30).…”

Purification and Characterization of an Immunogenic Aminopeptidase ofBrucella melitensis

“…Aminopeptidases (APEs) of many bacteria have been studied with some detail both structurally and enzymatically (2,17,31). On the other hand, it has been observed that interleukin-2 and gamma interferon are rapidly inactivated and degraded by proteinases from Pseudomonas aeruginosa and Legionella pneumophila (10,24).…”