کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
3136123 1195444 2016 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Exopeptidases and gingipains in Porphyromonas gingivalis as prerequisites for its amino acid metabolism
موضوعات مرتبط
علوم پزشکی و سلامت پزشکی و دندانپزشکی دندانپزشکی، جراحی دهان و پزشکی
پیش نمایش صفحه اول مقاله
Exopeptidases and gingipains in Porphyromonas gingivalis as prerequisites for its amino acid metabolism
چکیده انگلیسی

SummaryPorphyromonas gingivalis, an asaccharolytic bacterium, utilizes amino acids as energy and carbon sources. Since amino acids are incorporated into the bacterial cells mainly as di- and tri-peptides, exopeptidases including dipeptidyl-peptidase (DPP) and tripeptidyl-peptidase are considered to be prerequisite components for their metabolism. We recently discovered DPP11, DPP5, and acylpeptidyl oligopeptidase in addition to previously reported DPP4, DPP7, and prolyl tripeptidyl peptidase A. DPP11 is a novel enzyme specific for acidic P1 residues (Asp and Glu) and distributed ubiquitously in eubacteria, while DPP5 is preferential for the hydrophobic P1 residue and the first entity identified in prokaryotes. Recently, acylpeptidyl oligopeptidase with a preference for hydrophobic P1 residues was found to release N-terminally blocked di- and tri-peptides. Furthermore, we also demonstrated that gingipains R and K contribute to P1-basic dipeptide production. These observations implicate that most, if not all, combinations of di- and tri-peptides are produced from extracellular oligopeptides even with an N-terminal modification. Here, we review P. gingivalis exopeptidases mainly in regard to their enzymatic characteristics. These exopeptidases with various substrate specificities benefit P. gingivalis for obtaining energy and carbon sources from the nutritionally limited subgingival environment.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Japanese Dental Science Review - Volume 52, Issue 1, February 2016, Pages 22–29
نویسندگان
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