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The Reaction Coordinate of a Bacterial GH47 α‐Mannosidase: A Combined Quantum Mechanical and Structural Approach
Author(s) -
Thompson Andrew J.,
Dabin Jerome,
IglesiasFernández Javier,
Ardèvol Albert,
Dinev Zoran,
Williams Spencer J.,
Bande Omprakash,
Siriwardena Aloysius,
Moreland Carl,
Hu TingChou,
Smith David K.,
Gilbert Harry J.,
Rovira Carme,
Davies Gideon J.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201205338
Subject(s) - reaction coordinate , chemistry , mannosidase , substrate (aquarium) , mannose , enzyme , quantum , iminosugar , hydrolysis , nanotechnology , computational chemistry , stereochemistry , materials science , physics , biochemistry , biology , ecology , quantum mechanics
Mannosides in the southern hemisphere : Conformational analysis of enzymatic mannoside hydrolysis informs strategies for enzyme inhibition and inspires solutions to mannoside synthesis. Atomic resolution structures along the reaction coordinate of an inverting α‐mannosidase show how the enzyme distorts the substrate and transition state. QM/MM calculations reveal how the free energy landscape of isolated α‐ D ‐mannose is molded on enzyme to only allow one conformationally accessible reaction coordinate.