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Aminopeptidase activity of Capnocytophaga
Author(s) -
Nakamura Masakazu,
Slots Jøorgen
Publication year - 1982
Publication title -
journal of periodontal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.31
H-Index - 83
eISSN - 1600-0765
pISSN - 0022-3484
DOI - 10.1111/j.1600-0765.1982.tb01181.x
Subject(s) - aminopeptidase , capnocytophaga , biochemistry , microbiology and biotechnology , tripeptide , flavobacteriaceae , chemistry , leucine , valine , biology , amino acid , bacteria , 16s ribosomal rna , gene , genetics , bacteroidetes
Studies have shown that Capnocytophaga species are unique among the periodonlal microorganisms so far tested in that they produce marked leucine aminopeptidase, valine aminopeptidase, and cystine aminopeptidase activities. In this paper, we used the expanded API ZYMAP (API‐System, La Balme les Grottes, France) system to survey 18 Capnocytophaga strains for their ability to hydrolyze 57 synthetic substrates of β‐naphthylamide derivalives of amino acids, dipeplides, tripeptides, tetrapeptides, and pentapeptides. In general, the study strains exhibited marked hydroiylic activity against all test β‐naphthylamides bearing a free N‐terminal α‐amino group, The hydrolytic activity varied little among the strains. Since aminopeptidases can be involved in bradykinin formation and degradation of collagen fragments and other events ofthe inflammatory process, the Capnocytophaga aminopeptidases may be important virulence factors in Capnocytophaga ‐associated periodonial diseases.