Structural basis for cyclophellitol inhibition of a β-glucosidase

Tracey M. Gloster; Robert Madsen; Gideon J. Davies

doi:10.1039/b616590g

Structural basis for cyclophellitol inhibition of a β-glucosidase

Tracey M. Gloster, Robert Madsen, Gideon J. Davies

Department of Chemistry

University of York

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

The structural basis for b-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry. The natural product was shown to bind by a covalent bond in the active site of the enzyme. This bond is formed by ring-opening of the epoxide in cyclophellitol with a carboxylic acid from the enzyme.

Original language	English
Journal	Organic and Biomolecular Chemistry
Volume	5
Issue number	3
Pages (from-to)	444-446
ISSN	1477-0520
DOIs	https://doi.org/10.1039/b616590g
Publication status	Published - 2007

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title = "Structural basis for cyclophellitol inhibition of a β-glucosidase",

abstract = "The structural basis for b-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry. The natural product was shown to bind by a covalent bond in the active site of the enzyme. This bond is formed by ring-opening of the epoxide in cyclophellitol with a carboxylic acid from the enzyme.",

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T1 - Structural basis for cyclophellitol inhibition of a β-glucosidase

AU - Gloster, Tracey M.

AU - Madsen, Robert

AU - Davies, Gideon J.

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N2 - The structural basis for b-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry. The natural product was shown to bind by a covalent bond in the active site of the enzyme. This bond is formed by ring-opening of the epoxide in cyclophellitol with a carboxylic acid from the enzyme.

AB - The structural basis for b-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry. The natural product was shown to bind by a covalent bond in the active site of the enzyme. This bond is formed by ring-opening of the epoxide in cyclophellitol with a carboxylic acid from the enzyme.

U2 - 10.1039/b616590g

DO - 10.1039/b616590g

M3 - Journal article

C2 - 17252125

SN - 1477-0520

VL - 5

SP - 444

EP - 446

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 3

ER -

Structural basis for cyclophellitol inhibition of a β-glucosidase

Abstract

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