Aug 22, 2016 · Kcat = turnover of substrate to product / unit time. Kcat/Km = measure of catalytic efficiency. You use this if the question is asking about which enzyme has the greatest efficiency. Also may be given Vmax and enzyme concentration and asked to solve for Kcat, which would just be Vmax/[E] = Kcat

Aug 12, 2020 · The [S] terms cancel, which is why at saturating conditions, Vo = Vmax. Since kcat is a decent surrogate for Vmax here, what this means is that kcat tells us roughly how well the enzyme does when there's a lot of substrate around. In other words, the higher the kcat, the faster the reaction at high substrate concentrations.

Jul 11, 2021 · Vmax =Kcat[E] Catalytic efficiency = Kcat/Km *greater this value, more efficient the enzyme Hill coefficient > 1, positive cooperative binding Hill coefficient < 1, negative cooperative binding Hill coefficient = 1, no cooperative binding 5) V = E x z/f *migrational velocity = electric field x net charge/frictional coefficient

Aug 7, 2019 · Thinking about what Kcat is helps me remember how to calculate it. Kcat as the turnover constant describes the max amount of product formed per enzyme, per second. If you put that into units, that’s product/[E]*s, or Vmax/[E]. Hope this helps :) In your case [product]/s would be Vmax, where s is seconds or time, right?

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Aug 22, 2017 · Kcat is the number of substrate molecules/time that a enzyme can do. It's the turnover number. Km is the affinity an enzyme has for a substrate. It is measured as being the substrate concentration when the reaction is at 1/2 Vmax. REMEMBER: The higher the Km, the less affinity it has (bc it implies you need MORE substrate to reach the Vmax.

May 23, 2020 · Kcat is a ratio, and we know that Vmax and total enzyme concentration are directly proportional to one another. This means that if you double total enzyme conc, you will double Vmax. Thus, since kcat is a ratio of the two, when you increase both the numerator and denominator by the same factor, you have no change to the overall fraction.

May 25, 2021 · 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.

May 2, 2022 · Kcat describes catalysis higher Kcat means better catalysis. Km is kinda weird but you can kinda think of it has the warm up time. The bigger the Km that more substrate that enzyme needs to “warm-up” hence higher Km indicating lower affinity because you needed more substrate around to get going.

Nov 15, 2019 · What would be the Kcat (turnover number or molecular activity) of the enzyme under these conditions? I started by laying out everything I know: Kcat = Vmax/[E] in s-1 or min-1. 1 µg of enzyme = 1x10-6 g of enzyme Moles of E = mass/molar mass = 1x10-6 g/120,000 g/mol = 8.33333 x 10-12 moles of E Vmax = (2.75x10-6) mol/min