机械变形增强了结晶羧肽酶A的催化活性。
Mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A.
作者信息
Zenchenko T A, Morozov V N
机构信息
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region.
出版信息
Protein Sci. 1995 Feb;4(2):251-7. doi: 10.1002/pro.5560040211.
Abstract
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.
摘要
描述了一种研究酶中机械化学相互作用的新方法。已测量了经受单轴变形的结晶交联酶的催化活性。沿[010]方向延伸羧肽酶A的单斜P2(1)晶体，导致催化酯酶活性增加许多倍，而有效米氏常数没有变化。这种增加被解释为是由于与变形晶体中酶的催化活性相关的构象流动性的释放。
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