Molecular Basis for β‐Glucosidase Inhibition by Ring‐Modified Calystegine Analogues | Zendy

Aguilar Matilde | Zendy; Gloster Tracey M. | Zendy; GarcíaMoreno M. Isabel | Zendy; Ortiz Mellet Carmen | Zendy; Davies Gideon J. | Zendy; Llebaria Amadeu | Zendy; Casas Josefina | Zendy; EgidoGabás Meritxell | Zendy; García Fernandez José M. | Zendy

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Molecular Basis for β‐Glucosidase Inhibition by Ring‐Modified Calystegine Analogues

Author(s) -

Aguilar Matilde,

Gloster Tracey M.,

GarcíaMoreno M. Isabel,

Ortiz Mellet Carmen,

Davies Gideon J.,

Llebaria Amadeu,

Casas Josefina,

EgidoGabás Meritxell,

García Fernandez José M.

Publication year - 2008

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200800451

Subject(s) - thermotoga maritima , stereochemistry , chemistry , ring (chemistry) , derivative (finance) , alkaloid , biochemistry , organic chemistry , gene , escherichia coli , financial economics , economics

Neutral calystegine B 2 analogues , such as the 1‐deoxy‐6‐oxa‐ N ‐( N′ ‐octyl)thiocarbamoyl derivative, proved to be more potent β‐glucosidase inhibitors than the natural alkaloid. Structural studies of the complex with a clan GH‐A β‐glucosidase from Thermotoga maritima showed a binding mode markedly different from that of the parent compound.

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