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. 1991 May 30;1078(1):117-20.
doi: 10.1016/0167-4838(91)90100-e.

Interaction of beta-cyclodextrin with the granular starch binding domain of glucoamylase

N J Belshaw  1 , G Williamson
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Interaction of beta-cyclodextrin with the granular starch binding domain of glucoamylase

N J Belshaw et al. Biochim Biophys Acta. .

Abstract

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 (Kd) for the second ligand of 1.68 microM. 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 (Ki) of 11.0 +/- 1.9 microM. The results show that beta-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.

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