Action of a thermostable trehalose synthase from Thermus aquaticus on sucrose

被引：8

作者：

Nishimoto, T ^{[1
]}

Nakada, T ^{[1
]}

Chaen, H ^{[1
]}

Fukuda, S ^{[1
]}

Sugimoto, T ^{[1
]}

Kurimoto, M ^{[1
]}

Tsujisaka, Y ^{[1
]}

机构：

[1] HAYASHIBARA INST CORP, OKAYAMA 700, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1997年 / 61卷 / 05期

关键词：

trehalose synthase; sucrose; trehalulose;

D O I：

10.1271/bbb.61.898

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A thermostable trehalose synthase from Thermus aquaticus ATCC 33923, which catalyzes the interconversion between maltose and trehalose by intramolecular transglucosylation, converted sucrose into trehalulose (1-O-alpha-D-glucopyranosyl-D-fructose). The trehalulose-forming activity of the enzyme was very low compared with that of maltose and trehalose, Kinetic studies showed that sucrose competitively inhibited the interconversion activity between maltose and trehalose, Consequently, these three substrates, maltose, trehalose, and sucrose, are thought to bind the same active site of trehalose synthase.

引用

页码：898 / 899

页数：2

共 8 条

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