(Q27643651)

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Structural basis for cyclophellitol inhibition of a beta-glucosidase

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Structural basis for cyclophellitol inhibition of a beta-glucosidase (English)

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Robert Madsen

2

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Gideon Davies

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Gideon J Davies

series ordinal

3

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author name string

Tracey M Gloster

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1

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publication date

7 February 2007

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published in

Organic and Biomolecular Chemistry

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volume

5

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issue

3

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page(s)

444-6

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cites work

Mapping the conformational itinerary of beta-glycosidases by X-ray crystallography

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A short synthesis of (+)-cyclophellitol

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21 January 2018

Cyclophellitol: a naturally occurring mechanism-based inactivator of beta-glucosidases.

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Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate

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Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: tyrosine is the catalytic nucleophile

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Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase

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21 January 2018

Substrate distortion by a beta-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state

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Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase

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21 January 2018

X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease

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21 January 2018

Iminosugar glycosidase inhibitors: structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycin to beta-glucosidases

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An extensively modified version of MolScript that includes greatly enhanced coloring capabilities

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Production, isolation and structure determination of a novel beta-glucosidase inhibitor, cyclophellitol, from Phellinus sp

1 reference

12 April 2024

https://opencitations.net/index/api/v1/citations/10.7164/ANTIBIOTICS.43.49

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(Q27643651)

Structural basis for cyclophellitol inhibition of a beta-glucosidase

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