A new approach to study of enzyme mechano-chemistry is proposed which is based on measuring of catalytic activity of crystalline cross-linked samples subject to uniaxial tension. Deformation of monoclinic P2(1) carboxypeptidase A crystals along [010] directions results in considerable increase of their esterase activity with no changes in the Michaelis constant. This can be explained as a consequence of considerable conformational changes accompanying the enzyme cycle.
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