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Substrate Distortion by a Lichenase Highlights the Different Conformational Itineraries Harnessed by Related Glycoside Hydrolases
Author(s) -
Money Victoria A.,
Smith Nicola L.,
Scaffidi Adrian,
Stick Robert V.,
Gilbert Harry J.,
Davies Gideon J.
Publication year - 2006
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.200600802
Subject(s) - reaction coordinate , distortion (music) , glycoside hydrolase , substrate (aquarium) , chemistry , enzyme , stereochemistry , biophysics , computational chemistry , materials science , biochemistry , biology , optoelectronics , amplifier , ecology , cmos
Pick‐a‐path : A series of enzymatic snapshots along the reaction coordinate of a lichenase (specific for gluco‐configured substrates) demonstrates that this enzyme uses a different reaction pathway, featuring a 1 S 3 → 4 H 3 → 4 C 1 migration, to that previously observed for the closely related mannanases.