Tousignant Audrey, Pelletier Joelle N
Département de Chimie, Université de Montréal, Montréal, Québec, H3C 3J7, Canada.
Chem Biol. 2004 Aug;11(8):1037-42. doi: 10.1016/j.chembiol.2004.06.007.
A relationship between molecular dynamics motions of noncatalytic residues and enzyme activity has recently been proposed. We present examples where mutations either near or distal from the active site residues modify internal enzyme motion with resulting modification of catalysis. A better understanding of internal protein motions correlated to catalysis will lead to a greater insight into enzyme function.
最近有人提出非催化残基的分子动力学运动与酶活性之间存在关联。我们给出了一些例子，其中活性位点残基附近或远处的突变会改变酶的内部运动，从而导致催化作用的改变。更好地理解与催化相关的蛋白质内部运动将有助于更深入地了解酶的功能。
