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Infection and Immunity, March 2000, p. 1176-1182, Vol. 68, No. 3
Institute of Molecular Biology, Jagiellonian
University, 31-120 Krakow, Poland,1 and
Department of Biochemistry and Molecular Biology, University of
Georgia, Athens, Georgia 306022
Received 13 September 1999/Returned for modification 27 October
1999/Accepted 26 November 1999
Porphyromonas gingivalis is an asaccharolytic and
anaerobic bacterium that possesses a complex proteolytic system which
is essential for its growth and evasion of host defense mechanisms. In
this report, we show the purification and characterization of prolyl
dipeptidyl peptidase IV (DPPIV) produced by this organism. The enzyme
was purified to homogeneity, and its enzymatic activity and biochemical
properties were investigated. P. gingivalis DPPIV, like its
human counterpart, is able to cleave the N terminus of synthetic
oligopeptides with sequences analogous to those of interleukins 1
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Emerging Family of Proline-Specific Peptidases of
Porphyromonas gingivalis: Purification and
Characterization of Serine Dipeptidyl Peptidase, a Structural
and Functional Homologue of Mammalian Prolyl Dipeptidyl
Peptidase IV

and 2. Additionally, this protease hydrolyzes biologically active
peptides including substance P, fibrin inhibitory peptide, and
-casomorphin. Southern blot analysis of genomic DNA isolated from
several P. gingivalis strains reveal that a single copy of the DPPIV gene was present in all strains tested.
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602. Phone: (706) 542-1713. Fax: (706) 542-3719. E-mail:
potempa{at}arches.uga.edu.
Present address: The Rockefeller University, New York, NY 10021.
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