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Originally published In Press as doi:10.1074/jbc.M008789200 on November 28, 2000

J. Biol. Chem., Vol. 276, Issue 9, 6299-6305, March 2, 2001
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Porphyromonas gingivalis DPP-7 Represents a Novel Type of Dipeptidylpeptidase*

Agnieszka BanbulaDagger §, Jane YenDagger , Aneta OleksyDagger §, Pawel Mak§, Marcin BugnoDagger §, James TravisDagger , and Jan PotempaDagger §

From the Dagger  Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and the § Institute of Molecular Biology, Jagiellonian University, 34-120 Krakow, Poland

A novel dipeptidylpeptidase (DPP-7) was purified from the membrane fraction of Porphyromonas gingivalis. This enzyme, with an apparent molecular mass of 76 kDa, has the specificity for both aliphatic and aromatic residues in the P1 position. Although it belongs to the serine class of peptidases, it does not resemble other known dipeptidylpeptidases. Interestingly, the amino acid sequence around the putative active site serine residue shows significant similarity to the C-terminal region of the Staphylococcus aureus V-8 endopeptidase. The genes encoding homologues of DPP-7 were found in genomes of Xylella fastidiosa, Shewanella putrefaciens, and P. gingivalis. It is likely that at least in P. gingivalis, DPP-7 and its homologue, in concert with other di- and tripeptidases, serve nutritional functions by providing dipeptides to this asaccharolytic bacterium.

* This work was supported by National Institutes of Health Grant DE 09761 and by Committee of Scientific Research (KBN, Poland) Grant 6PO4A 047 17.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 706-542-1713; Fax: 706-542-3719; E-mail: potempa@arches.uga.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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