What is kcat

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Create a free Team What is Teams? Learn more. Ask Question. Asked 4 years, 11 months ago. Active 4 years, 11 months ago. Viewed 45k times. K m , the substrate concentration at which the reaction rate is half of V max K cat , used to describe the limiting rate of any enzyme-catalyzed reaction at saturation. Improve this question. KingBoomie KingBoomie 2, 2 2 gold badges 16 16 silver badges 39 39 bronze badges. Add a comment.

Active Oldest Votes. Improve this answer. Vmax is the maximum enzyme velocity in the same units as Y. It is not directly shown in the model above. It is the velocity of the enzyme extrapolated to very high concentrations of substrate, so is almost always higher than any velocity measured in your experiment. It is computed by multiplying Et times kcat.

The curve shown above is identical to the curve defined by the Michaelis-Menten model. You'll get identical curves when you fit either model to your data, and identical values for Km. The Michaelis-Menten model finds the Vmax, which is the maximum enzyme velocity extrapolated out to very high concentrations of substrate.

It is expressed in the same units you used to enter your Y values enzyme activity. The Vmax is determined by how many enzyme sites are present Et and the rate at which the enzyme can convert substrate to product kcat. If you know the concentration of enzyme sites you've added to the assay Et then you can fit the catalytic constant Kcat using the model above. When calculating Kcat, the concentration units cancel out, so Kcat is expressed in units of inverse time. It is the turnover number -- the number of substrate molecule each enzyme site converts to product per unit time.

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