Oct 1, 2024 · The ratio of kcat to Km (kcat/Km) is an important measure of an enzyme’s efficiency. It combines the rate of catalysis and the affinity of the enzyme for its substrate, providing a …

Km is a substrate concentration and is the amount of substrate it takes for an enzyme to reach V max /2. On the other hand V max /2 is a velocity and is nothing more than that. The value of …

All you have to do is find the [Et]. This is basically the total "Moles" of the enzymes you have used. which comes out to be 10^-10. Then you find the kcat = Vm/[Et], then find kcat/km

Jan 21, 2025 · Under these conditions the reaction is zero-order in substrate and we can use Vmax to calculate the enzyme’s concentration, typically using a variable-time method. At lower …

As a beginner, you may find it easier to use Eisenthal & Cornish-Bowden's "direct linear plot" of your data to determine Vmax and Km than a regression of v against [S]. As a non-parametric...

Nov 15, 2019 · In assays using 1 µg of enzyme per assay the Km was 3x10-3 M and the Vmax was 2.75 µmol per minute. What would be the Kcat (turnover number or molecular activity) of …

Nov 19, 2016 · Just as kcat k c a t represents the rate of reaction at saturating substrate concentration, kcat/Km k c a t / K m represents the rate of the reaction at negligible substrate …

Jun 13, 2022 · Although the parameter provides critical information on how the enzyme lowers the energy barriers along the reaction pathway for catalysis, kcat / KM is frequently considered as …

Out of all the mutations, it’s evident that the E162L has the most drastic increase in the enzyme’s Km (indicating low binding affinity) and the most drastic decrease in kcat (which means a …

Dec 27, 2020 · The kcat equation, also known as the Michaelis-Menten equation, lets you figure out how fast a reaction occurs with a catalyst. Make sure to use appropriate kcat units so you …