Kcat/Km就可以用来确定酶的最适底物，同一个酶对不同底物的Kcat/Km最大可相差100万倍。 当利用蛋白质工程对酶进行改造时，不同突变型的Kcat/Km也是需要测定的参数，用来表征酶催化效率的变化情况。

2020年7月11日 · So the slope is the inverse of kcat/km. Efficiency is Kcat/Km. Where the x intercept is 1/Km and the y intercept is 1/Vmax. You can't get the efficiency directly from the graph, but you could find Km and Vmax and then use Kcat=vmax/E. I …

2016年11月19日 · Kcat, used to describe the limiting rate of any enzyme-catalyzed reaction at saturation. Most of the time K cat just equals K 2 (NOT the case when there are more reaction steps)

2025年1月21日 · The catalytic rate kcat k c a t is the rate of product formation when the enzyme is saturated with substrate and therefore reflects the enzyme's maximum rate. The rate of product formation is dependent on both how well the enzyme binds substrate and how fast the enzyme converts substrate into product once substrate is bound.

Computing Kcat by hand. If you plot enzyme velocity as a function of subtrate concentration, you can fit the data to the Michaelis-Menten equation to determine the K m and V max. The V max is the maximum enzyme velocity extrapolated out to very high concentrations of substrate.

2024年8月31日 · The Lineweaver-Burk plot not only helps us determine kcat and Km but also provides insights into enzyme specificity and catalytic efficiency. By comparing the plots for different enzymes acting on the same substrate, we can understand which enzyme has a higher affinity (lower Km) and a faster turnover rate (higher kcat).

Notice k2 k 2 describes an irreversible reaction as opposed to an equilibrium expression, when compared to k-1 and k1. k2 here is also known as kcat, the catalytic efficiency of enzyme.

Kcat is the turnover number -- the number of substrate molecule each enzyme site converts to product per unit time. If you know the concentration of enzyme sites, you can fit Kcat instead of Vmax when analyzing a substrate vs. velocity curve.

2021年5月25日 · The definition of catalytic efficiency is kcat/Km. So to have a high catalytic efficiency, you want a large numerator (large kcat) and/or a small denominator (small Km). Conceptually, this shows the slope of a Michaelis-Menten curve at low substrate concentrations. I can show you the math on that if you want.

2022年4月8日 · No. A high kcat and a low Km = high catalytic efficiency. Which means it’s a better enzyme the more steep the slope is. Think about it like this: •a low Km means that the enzyme can bind very well to the substrate because the enzyme have a stronger affinity for the substrate. (i.e, enzyme has wants to bind substrate)