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Fructosyltransferase activity of a glucan-binding protein from Streptococcus mutans.
- Source :
-
Journal of general microbiology [J Gen Microbiol] 1983 Oct; Vol. 129 (10), pp. 3243-50. - Publication Year :
- 1983
-
Abstract
- Streptococcus mutans serotype c produces several extracellular proteins which bind to affinity columns of immobilized glucans. The proteins are three distinct glucosyltransferases and another glucan-binding protein (molecular weight 74000) which is now shown to be a fructosyltransferase. This enzyme is antigenically distinct and genetically independent of two other fructosyltransferases produced by the same organism. A mutant is described which lacks the glucan binding fructosyltransferase and has defective ability to form adherent colonies in the presence of sucrose. Although the production of glucans from sucrose results in the glucan binding protein becoming bound to the bacterial surface, and hence perhaps contributing to adherence, the fructans synthesized by the enzyme do not appear to contribute to this phenomenon.
- Subjects :
- Carrier Proteins genetics
Carrier Proteins isolation & purification
Glucosyltransferases isolation & purification
Hexosyltransferases genetics
Hexosyltransferases isolation & purification
Molecular Weight
Mutation
Protein Binding
Serotyping
Streptococcus mutans genetics
Carrier Proteins metabolism
Glucans metabolism
Hexosyltransferases metabolism
Streptococcus mutans enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1287
- Volume :
- 129
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Journal of general microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 6228637
- Full Text :
- https://doi.org/10.1099/00221287-129-10-3243