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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.
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
URL: http://dx.doi.org/10.1159/000065962
DOI: 10.1159/000065962
PubMed id: 12399696
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