[The effect of deformation on the catalytic activity of carboxypeptidase A in the crystalline state].
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.
Zenchenko
T A
TA
Morozov
V N
VN
D002268:Carboxypeptidases / Q000737:chemistry / Q000378:metabolism*; D043422:Carboxypeptidases A; D002384:Catalysis; D003460:Crystallization; D011487:Protein Conformation
D002268:Carboxypeptidases; D043422:Carboxypeptidases A
Vliianie deformatsii na kataliticheskuiu aktivnost' karboksipeptidazy A v kristallicheskom sostoianii.