Marangoni A G
Guelph-Waterloo Center for Graduate Work in Chemistry, Department of Food Science, University of Guelph, ON, Canada.
Biochem Biophys Res Commun. 1994 May 16;200(3):1321-8. doi: 10.1006/bbrc.1994.1595.
A model for the enzyme kinetics of lipolysis was developed where the rate limiting step of the reaction is the interfacial binding step. Binding involves the association of the enzyme with a cluster of substrate molecules and a conformational change in the enzyme, resulting in an interfacially penetrated lipase bound to a cluster of substrate molecules. The resulting derived rate equation is identical to the HIll equation. Fits of the model to experimental velocity vs. substrate concentration data from the literature allowed for the determination of enzyme-substrate interface dissociation constants and reaction order with respect to substrate concentration.
建立了一种脂肪分解酶动力学模型，其中反应的限速步骤是界面结合步骤。结合涉及酶与底物分子簇的缔合以及酶的构象变化，导致界面渗透的脂肪酶与底物分子簇结合。由此得出的速率方程与希尔方程相同。将该模型与文献中的实验速度与底物浓度数据进行拟合，可以确定酶-底物界面解离常数以及相对于底物浓度的反应级数。
