Porphyromonas gingivalis DPP-7 Represents a Novel Type of Dipeptidylpeptidase

• Published in: The Journal of biological chemistry Vol. 276; no. 9; pp. 6299 - 6305
• Main Authors: Banbula, Agnieszka, Yen, Jane, Oleksy, Aneta, Mak, Pawel, Bugno, Marcin, Travis, James, Potempa, Jan
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 02.03.2001; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Base Sequence; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - antagonists & inhibitors; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - metabolism; dipeptidylpeptidase; DPP-7 protein; Enzyme Stability; Hydrogen-Ion Concentration; Molecular Sequence Data; Porphyromonas gingivalis; Porphyromonas gingivalis - enzymology; Substrate Specificity
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M008789200

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 theStaphylococcus aureus V-8 endopeptidase. The genes encoding homologues of DPP-7 were found in genomes of Xylella fastidiosa, Shewanella putrefaciens, andP. 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.