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Papers In Press, published online ahead of print November 28, 2000
J. Biol. Chem, 10.1074/jbc.M008789200
Submitted on September 26, 2000
Revised on November 28, 2000
Accepted on November 28, 2000

Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase

Agnieszka Banbula, Jane Yen, Aneta Oleksy, Pawel Mak, Marcin Bugno, James Travis, and Jan Potempa

Biochem & Mol Biol, University of Georgia, Athens, GA 30602

Corresponding Author: potempa{at}arches.uga.edu

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 homology to the C-terminal region of the Staphylococcus aureus V-8 endopeptidase. In P. gingivalis, DPP-7 probably serves nutritional functions by providing dipeptides to this assaccharolytic bacterium.


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Y.-Y. Chen, K. J. Cross, R. A. Paolini, J. E. Fielding, N. Slakeski, and E. C. Reynolds
CPG70 Is a Novel Basic Metallocarboxypeptidase with C-terminal Polycystic Kidney Disease Domains from Porphyromonas gingivalis
J. Biol. Chem., June 21, 2002; 277(26): 23433 - 23440.
[Abstract] [Full Text] [PDF]


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