A novel glucosyltransferase from Streptococcus mutans produces oligo-isomaltosaccharides.
Streptococcus mutans secretes a sucrose-independent branalphang enzyme that utilizes isomaltosaccharides as donors for branalphang formation on dextran. Although the branching enzyme is necessary for the formation of extracellular polysaccharide complexes, the source of the donor for the enzyme is unknown. In this study, we purified a novel glucosyltransferase from S. mutans and characterized its properties. The glucosyltransferase was primer independent 1,6-alpha-D-glucan synthase, which produced oligo-isomaltosaccharides. The enzyme was thought to be a source of donor for the branching enzyme in S. mutans.
D004187:Disaccharides / Q000096:biosynthesis*; D005964:Glucosyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D005779:Immunodiffusion; D007534:Isomaltose / Q000096:biosynthesis*; D007700:Kinetics; D009844:Oligosaccharides / Q000096:biosynthesis*; D013295:Streptococcus mutans / Q000201:enzymology*
D004187:Disaccharides; D009844:Oligosaccharides; D007534:Isomaltose; D005964:Glucosyltransferases; C040232:glucan synthase