IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Banbula, A.
Right arrow Articles by Potempa, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Banbula, A.
Right arrow Articles by Potempa, J.

 Previous Article  |  Next Article 

Infection and Immunity, March 2000, p. 1176-1182, Vol. 68, No. 3
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

Agnieszka Banbula,1 Marcin Bugno,1 Jason Goldstein,2 Jane Yen,2 Daniel Nelson,2,dagger James Travis,2 and Jan Potempa1,2,*

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 1beta and 2. Additionally, this protease hydrolyzes biologically active peptides including substance P, fibrin inhibitory peptide, and beta -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.

dagger Present address: The Rockefeller University, New York, NY 10021.


Infection and Immunity, March 2000, p. 1176-1182, Vol. 68, No. 3
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2000 by the American Society for Microbiology. All rights reserved.