What is the meaning behind Kcat / Km? - Biology Stack Exchange
Nov 19, 2016 · I'm trying to understand enzyme kinetics, the formula for Km and Kcat make sense to me. Km , the substrate concentration at which the reaction rate is half of Vmax Kcat, used to …
kcat in uncompetitive enzyme inhibition - Biology Stack Exchange
Jul 30, 2020 · Mathematically, kcat = Vmax [E] k cat = V max [E] (where [E] [E] is the concentration of enzyme, excluding that which has been inactivated by inhibitor). Now, …
biochemistry - Michaelis-Menten equation; how to find the …
I was wondering what the constants in the Michaelis-Menten equation actually mean in experimental data of enzymes. How do I process the data to find Km and Kcat? I did an …
How to calculate the turnover number? - Biology Stack Exchange
I understand that Kcat (turnover number) = Vmax/total enzyme concentration. However the formula I have been given is Kcat = specific activity/molecular mass of enzyme. What is the …
Is there any way to estimate the kcat of an enzyme if we don't …
Jan 31, 2025 · Is there a way to estimate the kcat of an enzyme using a kinetic assay if we don't know the enzyme concentration? I thought that perhaps one could fit the Michaelis-Menten …
In what cases can $k_{\\rm cat}/K_{\\rm M}$ be used to compare ...
May 29, 2024 · The ratio kcat/KM k c a t / K M is often used to compare the catalytic efficiency of enzymes, but this paper has suggested that kcat/KM k c a t / K M should be abandoned for …
Why does uncompetitive inhibition decrease the Michaelis constant?
Jun 27, 2016 · uncompetitive At negligible substrate concentrations, the amount of substrate bound enzyme (and the effect of inhibition) is negligible. Thus the rate should be the same …
Enzyme kinetics: Effect of immobilization on kinetic parameters
Mar 21, 2016 · What is the typical effect of enzyme immobilization on the kinetic parameters of an enzyme's activity? Can one assume that they'd stay approximately the same or is there a …
What are the structural factors affect enzyme's Km?
So, any mutation that for example disrupts an H-bond between the enzyme and its substrate would increase KM. Any mutation that targets a catalytic residue (say, an amino-acid side …
Effect of pH, temperature and enzyme concentration on Km
Jan 2, 2022 · Another issue which makes me think so: In all the biochemistry literature that I have encountered Km and Kcat appears for each enzyme with no indication of the temperature or …