Evidence for the presence of two distinct sites of sucrose hydrolysis and glucosyl transfer activities on 1,3-α-D-glucan synthase of Streptococcus mutans

Yoshihisa Yamashita, N. Hanada, M. Itoh-Andoh, T. Takehara

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抄録

1,3-α-D-Glucan synthase of Streptococcus mutans catalyzes both the hydrolysis of sucrose to glucose and fructose, and the glucosyl transfer to glucosyl polymers to yield water-insoluble glucan. The enzyme catalyzes only sucrose hydrolysis, however, in the absence of 1,6-α-D-glucan as an acceptor. In the present study, we found that glucosyl transfer activity was completely inhibited by the antiserum against isolated 1,3-α-D-glucan synthase but that the sucrose hydrolysis activity was not. The antiserum did not impair the binding of the enzyme to the acceptor. These findings indicate that sucrose hydrolysis and glucosyl transfer occur at two distinct sites on the enzyme.

元の言語英語
ページ(範囲)343-346
ページ数4
ジャーナルFEBS Letters
243
発行部数2
DOI
出版物ステータス出版済み - 1 30 1989

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Streptococcus mutans
Sucrose
Hydrolysis
Immune Sera
Enzymes
Glucans
Fructose
Polymers
Glucose
polyglucosan
glucan synthase
Water

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

これを引用

Evidence for the presence of two distinct sites of sucrose hydrolysis and glucosyl transfer activities on 1,3-α-D-glucan synthase of Streptococcus mutans. / Yamashita, Yoshihisa; Hanada, N.; Itoh-Andoh, M.; Takehara, T.

:: FEBS Letters, 巻 243, 番号 2, 30.01.1989, p. 343-346.

研究成果: ジャーナルへの寄稿記事

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AB - 1,3-α-D-Glucan synthase of Streptococcus mutans catalyzes both the hydrolysis of sucrose to glucose and fructose, and the glucosyl transfer to glucosyl polymers to yield water-insoluble glucan. The enzyme catalyzes only sucrose hydrolysis, however, in the absence of 1,6-α-D-glucan as an acceptor. In the present study, we found that glucosyl transfer activity was completely inhibited by the antiserum against isolated 1,3-α-D-glucan synthase but that the sucrose hydrolysis activity was not. The antiserum did not impair the binding of the enzyme to the acceptor. These findings indicate that sucrose hydrolysis and glucosyl transfer occur at two distinct sites on the enzyme.

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