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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)343-346
Number of pages4
JournalFEBS Letters
Volume243
Issue number2
DOIs
Publication statusPublished - Jan 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

Cite this

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.

In: FEBS Letters, Vol. 243, No. 2, 30.01.1989, p. 343-346.

Research output: Contribution to journalArticle

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