What is competitive Inhibition?
In competitive inhibition, the substrate and inhibitor cannot bind to the enzyme at the same time, as shown in the figure on the right. This usually results from the inhibitor having an affinity for the active site of an enzyme where the substrate also binds; the substrate and inhibitor compete for access to the enzyme's active site. This type of inhibition can be overcome by sufficiently high concentrations of substrate (Vmax remains constant), i.e., by out-competing the inhibitor. However, the apparent Km will increase as it takes a higher concentration of the substrate to reach the Km point, or half the Vmax. Competitive inhibitors are often similar in structure to the real substrate.
How to Calculate Maximum Rate given Apparent Value of Michaelis Menten Constant?
Maximum Rate given Apparent Value of Michaelis Menten Constant calculator uses Maximum Rate = (Initial Reaction Rate*(Apparent Michaelis Constant+Substrate Concentration))/Substrate Concentration to calculate the Maximum Rate, The Maximum rate given apparent value of Michaelis Menten constant formula is defined as a plot of the reaction velocity (V0) associated with the concentration [S] of the substrate can then be used to determine values such as Vmax, initial velocity, and Km(app). Maximum Rate is denoted by Vmax symbol.
How to calculate Maximum Rate given Apparent Value of Michaelis Menten Constant using this online calculator? To use this online calculator for Maximum Rate given Apparent Value of Michaelis Menten Constant, enter Initial Reaction Rate (V0), Apparent Michaelis Constant (Kmapp) & Substrate Concentration (S) and hit the calculate button. Here is how the Maximum Rate given Apparent Value of Michaelis Menten Constant calculation can be explained with given input values -> 0.00405 = (450*(12000+1500))/1500.