2016年11月19日 · The kcat/Km ratio doesn't represent something real, it's just a lazy way to compare enzymes, combining two numbers that each represent something different into one number that's only looking good because it's one number.

2017年6月11日 · Km is a particular "equilibrium constant" which stands for Michaelis-Menton constant. You will usually see this for enzyme kinetics, more specifically on graphs relating substrate concentration to velocity of enzyme.

2020年8月12日 · Kcat is the turnover number for an enzyme. It’s a measure of how fast the enzyme goes from Enzyme + (bound) Substrate to Enzyme + Product (ES —> E + P). Another way to think of it is a measure of how many substrate molecules are converted to product molecules per unit time. Mathematically, it’s defined as Kcat = Vmax/ [Enzyme]. Catalytic efficiency, or Kcat/Km, is a measure of an enzyme ...

2016年8月22日 · 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 Km can be used for a substrates affinity to the enzyme. lower Km=higher affinity. Eg.

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. An enzyme is said to be efficient if it doesn't take much substrate to get a fast ...

2015年3月3日 · A high Km means that you need more substrate to reach a certain reaction rate, while a low Km means the opposite. Kcat, or k2 or turnover number (they all mean the same thing) is a measure of how many substrates one (1) enzyme can convert into a product per second. Vmax is simply Kcat times the enzyme concentration.

2017年8月22日 · Catalytic efficiency is Kcat/Km. Not really a formal definition, but just a definition that kinetics experiments use as it incorporates both the turnover (the reaction) and the binding of the enzyme for substrate (the affinity), both which are important to enzyme efficiency.

2024年3月20日 · Km is defined as (k1 + kcat)/k-1 where k1 is the forward rate constant for the binding of substrate to enzyme, and k-1 is the reverse rate constant. It doesn't tell you necessarily how fast the reaction gets to equilibrium.

2022年6月24日 · What exactly is the difference between the two terms and why would the differentiation be useful? Edit: So, if I’m understanding this correctly: vmax would be the highest rate of substrates changed in the system whereas kcat is the efficiency of an enzyme. I’d appreciate some thoughts on this.

2021年7月6日 · kcat is the speed of the ES—>E+P per enzyme Vmax is the rate when the enzyme is saturated with substrate Kd is the dissociation constant — an equilibrium constant describing complexes (for example, the Keq of [ ML<—>M + L ]) Km is the substrate concentration at half of Vmax