INTERACTION OF BETA-CYCLODEXTRIN WITH THE GRANULAR STARCH BINDING DOMAIN OF GLUCOAMYLASE

被引：39

作者：

BELSHAW, NJ ^{[1
]}

WILLIAMSON, G ^{[1
]}

机构：

[1] INST FOOD RES, NORWICH NR4 7UA, NORFOLK, ENGLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1991年 / 1078卷 / 01期

关键词：

GLUCOAMYLASE; CYCLODEXTRIN; STARCH; BINDING DOMAIN;

D O I：

10.1016/0167-4838(91)90100-E

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：

The granular starch binding domain of glucoamylase 1 (EC 3.2.1.3 1,4-alpha-D-glucan glucohydrolase) binds two molecules of beta-cyclodextrin, with a dissociation constant (K(d)) for the second ligand of 1.68-mu-M. The catalytic domain showed no interaction with beta-cyclodextrin. Beta-cyclodextrin competitively inhibited the adsorption of the binding domain onto granular starch with an inhibition constant (K(i)) of 11.0 +/- 1.9-mu-M. The results show that beta-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.

引用

页码：117 / 120

页数：4

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