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

Nigel  J. Belshaw; Gary Williamson

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

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

Nigel J. Belshaw
, Gary Williamson

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

37 Citations (Scopus)

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.

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

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

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.",

author = "Belshaw, \{Nigel J.\} and Gary Williamson",

year = "1991",

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day = "30",

doi = "10.1016/0167-4838(91)90100-e",

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volume = "1078",

pages = "117--120",

journal = "Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology",

issn = "0167-4838",

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T1 - Interaction of b-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 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.

AB - 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.

U2 - 10.1016/0167-4838(91)90100-e

DO - 10.1016/0167-4838(91)90100-e

M3 - Article

SN - 0167-4838

VL - 1078

SP - 117

EP - 120

JO - Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

JF - Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

IS - 1

ER -

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

Abstract

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