2016年11月19日 · With negligible substrate, all you have is free enzyme - there isn't enough substrate to have appreciable amounts of substrate-bound form, and the rate of enzyme-substrate encounter is much lower than the rate of product formation, meaning that in the steady state you don't have appreciable amounts of product-bound form, either.

2020年7月30日 · Aside from grammar and punctuation fixes, your question needs attention to the following issues: 1. Please mention the source of the information (kcat remaining unchanged in uncompetitive inhibition) and the context in which it was given. 2. 'enzyme–substrate work efficiency' is not a well defined term in biology. Can you word it better?

2016年3月21日 · kcat 0.5 1/min Km 0.6 microM [E0] 5 micro M [S] 60 micro M Could I expect to retain them after immobilization? Or are these too high for an immobilized enzyme? If it matters, it is a 500 residue enzyme with a MW of approx. 65,000 Da

However the formula I have been given is Kcat = specific activity/molecular mass of enzyme. What is the relationship between these two different formulas - why do they give the same answer? Definition of Kcat that I am using: specific activity * molecular mass of the enzyme Specific activity = units of enzyme/ mass of protein in mg

2025年1月31日 · 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 equation to a series of progress curves at different substrate levels, but then I realized the fit wouldn't be able to tease apart the product kcar*E.

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 experiment on catalase and its breakdown of hydrogen peroxide. I used a gas pressure sensor to track how much O2 was produced from the reaction over time.

2022年1月2日 · 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 pH for which those values were observed (not in Lehninger, nor Wikipedia or other textbooks). I have not been able to find a detailed consideration of this point.

2016年6月27日 · Enzyme inhibitors (even competitive ones ones) don't change the intrinsic binding affinity of the free enzyme to substrate. Instead, they draw off some of the enzyme from the productive pathway. Because they change the concentration of particular enzyme species, they change the observed rate equation.

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2012年10月23日 · This enzyme shows positive co-operativity with respect to its substrate glucose, and the authors develop a kinetic analysis in terms of various parameters. These include an S 0.5 value for glucose, but a K M value for ATP (presumably because the kinetics with respect to ATP are simple Michaelis-Menten).