A novel glucosyltransferase from Streptococus mutans produces oligo-isomaltosaccharides

Yoshihisa Yamashita; Nobuhiro Hanada; Tadamichi Takehara

doi:10.1016/0006-291X(88)90446-9

A novel glucosyltransferase from Streptococus mutans produces oligo-isomaltosaccharides

Yoshihisa Yamashita, Nobuhiro Hanada, Tadamichi Takehara

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

Streptococcus mutans secretes a sucrose-independent branching enzyme that utilizes isomaltosaccharides as donors for branching 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-α-D-glucan synthase, which produced oligo-isomaltosaccharides. The enzyme was thought to be a source of donor for the branching enzyme in S. mutans.

Original language	English
Pages (from-to)	687-693
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	150
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(88)90446-9
Publication status	Published - Jan 29 1988
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Biophysics
Molecular Biology

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abstract = "Streptococcus mutans secretes a sucrose-independent branching enzyme that utilizes isomaltosaccharides as donors for branching 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-α-D-glucan synthase, which produced oligo-isomaltosaccharides. The enzyme was thought to be a source of donor for the branching enzyme in S. mutans.",

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AU - Takehara, Tadamichi

PY - 1988/1/29

Y1 - 1988/1/29

N2 - Streptococcus mutans secretes a sucrose-independent branching enzyme that utilizes isomaltosaccharides as donors for branching 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-α-D-glucan synthase, which produced oligo-isomaltosaccharides. The enzyme was thought to be a source of donor for the branching enzyme in S. mutans.

AB - Streptococcus mutans secretes a sucrose-independent branching enzyme that utilizes isomaltosaccharides as donors for branching 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-α-D-glucan synthase, which produced oligo-isomaltosaccharides. The enzyme was thought to be a source of donor for the branching enzyme in S. mutans.

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