Fructosyltransferase Activity of a Glucan-binding Protein from Streptococcus mutans
- 1 October 1983
- journal article
- research article
- Published by Microbiology Society in Microbiology
- Vol. 129 (10) , 3243-3250
- https://doi.org/10.1099/00221287-129-10-3243
Abstract
S. mutans serotype c produces several extracellular proteins which bind to affinity columns of immobilized glucans. The proteins are 3 distinct glucosyltransferases and another glucan-binding protein (MW 74,000) which is now shown to be a fructosyltransferase. This enzyme is antigenically distinct and genetically independent of 2 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, perhaps contributing to adherence [and carcinogenicity], the fructans synthesized by the enzyme do not appear to contribute to this phenomenon.This publication has 2 references indexed in Scilit:
- Effect of Dextran and Ammonium Sulphate on the Reaction Catalysed by a Glucosyltransferase Complex from Streptococcus mutansMicrobiology, 1980
- The physical and enzymatic properties of a phytohemagglutinin from mung beansJournal of Biological Chemistry, 1978