publication . Other literature type . Article . 2014

Identification and Characterization of Prokaryotic Dipeptidyl-peptidase 5 from Porphyromonas gingivalis

Ohara-Nemoto, Yuko; Rouf, Shakh M. A.; Naito, Mariko; Yanase, Amie; Tetsuo, Fumi; Ono, Toshio; Kobayakawa, Takeshi; Shimoyama, Yu; Kimura, Shigenobu; Nakayama, Koji; ...
Open Access English
  • Published: 07 Jan 2014
  • Publisher: American Society for Biochemistry and Molecular Biology
Abstract
Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is one of the major causative organisms of chronic periodontitis. The bacterium utilizes amino acids as energy and carbon sources, and incorporates them mainly as dipeptides. Therefore, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. A DPP7-like activity still remained in a dpp4-7-11 disrupted P. gingivalis ATCC 33277. PGN_0756, currently annotated as a prolyl oligopeptidase, possessed an activity indistinguishable from that of the triple dpp ...
Subjects
free text keywords: Microbiology, DPP4, DPP5, DPP7, DPP11, substrate specificity, Cell Biology, Biochemistry, Molecular Biology, Peptide sequence, Oligopeptide, Mutant, Amino acid, chemistry.chemical_classification, chemistry, Fungal protein, Biology, Porphyromonas gingivalis, biology.organism_classification, Gingipain, Dipeptidyl peptidase
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publication . Other literature type . Article . 2014

Identification and Characterization of Prokaryotic Dipeptidyl-peptidase 5 from Porphyromonas gingivalis

Ohara-Nemoto, Yuko; Rouf, Shakh M. A.; Naito, Mariko; Yanase, Amie; Tetsuo, Fumi; Ono, Toshio; Kobayakawa, Takeshi; Shimoyama, Yu; Kimura, Shigenobu; Nakayama, Koji; ...