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An aminopeptidase nutritionally important to Fusobacterium nucleatum

Article Abstract:

Research was conducted to evaluate an aminopeptidase isolated from the chemostat-grown cells of Fusobacterium nucleatum. Results indicated that the absence of an inhibitory effect of bestatin and 1,10-phenanthroline on F. nucleatum's growth. EDTA-inactivated activity was restored by cobalt ions. Moreover, a peptidase was found to play an important role in the survival of F. nucleatum in a subgingival environment.

Author: Rogers, A.H., Gunadi, A., Gully, N.J., Zilm, P.S.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
Research, Bacteria, Aminopeptidases

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Topological investigations of the FomA porin from Fusobacterium nucleatum and identification of the constriction loop L6

Article Abstract:

Research reveals that deletions in the external region of loop L6 of the FomA porin of Fusobacterium nucleatum leads to larger pore size in the porin facilitating permeability of antibiotics and sugars. Despite sharing the common beta-barrel motiff with the rest of the porins, FomA porin exhibits some topological constraints.

Author: Puntervoll, Pal, Kleivdal, Hans, Jensen, Herald B.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
Analysis, Structure-activity relationships (Biochemistry), Bacterial proteins, Mutagenesis, Permeability

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The Fusobacterium nucleatum porin FomA possesses the general topology of the non-specific porins

Article Abstract:

Research reveals that porin FomA of Fusobacterium nucleatum is one of the major non-specific porins and exhibit a beta-barrel topology of the non-specific porins except that the third loop does not function as a constriction loop.

Author: Puntervoll, Pal, Kleivdal, Hans, Dahl, Karl Ole, Bitter, Wilbert, Tommassen, Jan, Jensen, Harald B.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2000
United Kingdom, Netherlands, Physiological aspects, Enzymes, Membrane proteins, Proteins, Cells, Cell permeability, Enzyme structure-activity relationships, Protein conformation

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Subjects list: Statistical Data Included, Norway
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