Mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A.
A new approach for investigating mechano-chemical interactions in enzymes is described. The catalytic activity of crystalline crosslinked enzymes subjected to uniaxial deformation has been measured. Extension of monoclinic P2(1) crystals of carboxypeptidase A along the [010] direction leads to a many-fold increase in catalytic esterase activity with no changes in the effective Michaelis constant. This increase is interpreted as due to liberation of conformational mobility associated with catalytic activity of the enzyme in the deformed crystal.
Zenchenko
T A
TA
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region.
Morozov
V N
VN
D002268:Carboxypeptidases / Q000737:chemistry / Q000378:metabolism*; D043422:Carboxypeptidases A; D003432:Cross-Linking Reagents / Q000494:pharmacology; D003460:Crystallization; D004950:Esterases / Q000037:antagonists & inhibitors / Q000378:metabolism; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D006626:Hippurates / Q000378:metabolism; D007700:Kinetics; D007773:Lactates / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics
D003432:Cross-Linking Reagents; D006146:Guanidines; D006626:Hippurates; D007773:Lactates; C066372:benzoylglycyl phenyllactate; D004950:Esterases; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D019791:Guanidine