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Inhibition of catalytic and glucan-binding activities of a streptococcal GTF forming insoluble glucans

Lookup NU author(s): Dr Craig Thelwell, Emeritus Professor Roy Russell


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The ability of a range of potential inhibitors to affect the catalytic activity or binding of dextran by a glucosyltransferase (GTF-I) that synthesises insoluble α.1,3-linked glucan was tested. Acarbose, deoxynojirimycin, N-dodecyl-deoxynojirimycin and Tris, which are thought to interfere with the active site of the enzyme of GTF and related glycosidases, inhibited glucan synthesis but not glucan binding. Tris was found to act as a competitive inhibitor of GTF-I. The effectiveness of the active site inhibitors was not altered by immobilisation of GTF-I on salivacoated hydroxyapatite. In contrast, three amine hydrofluorides were markedly less effective against immobilised GTF than soluble GTF. The pH of the reaction mixture was found to have a strong influence on inhibition by acarbose, Tris and amine hydrofluorides, a finding that is of direct relevance to use of inhibitors in vivo. Copynght © 2002 S. Karger AG, Basel.

Publication metadata

Author(s): Wright WG, Thelwell C, Svensson B, Russell RRB

Publication type: Article

Publication status: Published

Journal: Caries Research

Year: 2002

Volume: 36

Issue: 5

Pages: 353-359

Print publication date: 01/09/2002

ISSN (print): 0008-6568

ISSN (electronic): 1421-976X

Publisher: S. Karger AG


DOI: 10.1159/000065962

PubMed id: 12399696


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