Substrate Distortion by a Lichenase Highlights the Different Conformational Itineraries Harnessed by Related Glycoside Hydrolases | Zendy

Money Victoria A. | Zendy; Smith Nicola L. | Zendy; Scaffidi Adrian | Zendy; Stick Robert V. | Zendy; Gilbert Harry J. | Zendy; Davies Gideon J. | Zendy

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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.

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