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

Nigel J. Belshaw; Gary Williamson

doi:10.1016/0167-4838(91)90100-E

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

Nigel J. Belshaw, Gary Williamson

Research output: Contribution to journal › Article › Research › peer-review

37 Citations (Scopus)

Abstract

The granular starch binding domain of glucoamyla 1 (EC 3.2.1.3 1,4-α-d-glucan glucohydrolase) binds two molecules of β-cyclodextrin, with a dissociation constant (K_d) for the second ligand of 1.68 μM. The catalytic domain showed no interaction with β-cyclodextrin. β-cyclodextrin competitively inhibited the adsorption of the binding domain onto granular starch with an inhibition constant (K_i) of 11.0 ± 1.9 μM. The results show that β-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.

Original language	English
Pages (from-to)	117-120
Number of pages	4
Journal	Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume	1078
Issue number	1
DOIs	https://doi.org/10.1016/0167-4838(91)90100-E
Publication status	Published - 30 May 1991
Externally published	Yes

Keywords

Binding domain
Cyclodextrin
Glucoamylase
Starch

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10.1016/0167-4838(91)90100-E

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title = "Interaction of β-cyclodextrin with the granular starch binding domain of glucoamylase",

abstract = "The granular starch binding domain of glucoamyla 1 (EC 3.2.1.3 1,4-α-d-glucan glucohydrolase) binds two molecules of β-cyclodextrin, with a dissociation constant (Kd) for the second ligand of 1.68 μM. The catalytic domain showed no interaction with β-cyclodextrin. β-cyclodextrin competitively inhibited the adsorption of the binding domain onto granular starch with an inhibition constant (Ki) of 11.0 ± 1.9 μM. The results show that β-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.",

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T1 - Interaction of β-cyclodextrin with the granular starch binding domain of glucoamylase

AU - Belshaw, Nigel J.

AU - Williamson, Gary

PY - 1991/5/30

Y1 - 1991/5/30

N2 - The granular starch binding domain of glucoamyla 1 (EC 3.2.1.3 1,4-α-d-glucan glucohydrolase) binds two molecules of β-cyclodextrin, with a dissociation constant (Kd) for the second ligand of 1.68 μM. The catalytic domain showed no interaction with β-cyclodextrin. β-cyclodextrin competitively inhibited the adsorption of the binding domain onto granular starch with an inhibition constant (Ki) of 11.0 ± 1.9 μM. The results show that β-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.

AB - The granular starch binding domain of glucoamyla 1 (EC 3.2.1.3 1,4-α-d-glucan glucohydrolase) binds two molecules of β-cyclodextrin, with a dissociation constant (Kd) for the second ligand of 1.68 μM. The catalytic domain showed no interaction with β-cyclodextrin. β-cyclodextrin competitively inhibited the adsorption of the binding domain onto granular starch with an inhibition constant (Ki) of 11.0 ± 1.9 μM. The results show that β-cyclodextrin binds to the binding domain of glucoamylase at the same site(s) as granular starch.

KW - Binding domain

KW - Cyclodextrin

KW - Glucoamylase

KW - Starch

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

Abstract

Keywords

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