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Substrate Distortion by a β ‐Mannanase: Snapshots of the Michaelis and Covalent‐Intermediate Complexes Suggest a B 2,5 Conformation for the Transition State
Author(s) -
Ducros Valérie M.A.,
Zechel David L.,
Murshudov Garib N.,
Gilbert Harry J.,
Szabó Lóránd,
Stoll Dominik,
Withers Stephen G.,
Davies Gideon J.
Publication year - 2002
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 - 10.1002/1521-3773(20020802)41:15<2824::aid-anie2824>3.0.co;2-g
Subject(s) - chemistry , substrate (aquarium) , covalent bond , mannosidase , distortion (music) , stereochemistry , reaction coordinate , hydrolase , crystallography , conformational change , enzyme , materials science , computational chemistry , biochemistry , biology , organic chemistry , ecology , amplifier , cmos , optoelectronics
The conformational reaction pathway for β ‐mannosidases proposed here is distinct from that of glucosidases and cellulases. The proposal is based on substrate distortions along the reaction pathway of a β ‐mannosidase (see picture) that were revealed by X‐ray crystallography and are close in conformational space to known β ‐mannosidase inhibitors.