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 Modifying Factor in Michaelis Menten Equation?
Maximum Rate given Modifying Factor in Michaelis Menten Equation calculator uses Maximum Rate = (Initial Reaction Rate*((Enzyme Modifying Factor*Michaelis Constant)+(Enzyme Substrate Modifying Factor*Substrate Concentration)))/Substrate Concentration to calculate the Maximum Rate, The Maximum rate given modifying factor in Michaelis Menten equation formula is defined as the enzyme activity under various substrate and inhibitor concentrations, to obtain a modified Michaelis–Menten equation. Maximum Rate is denoted by Vmax symbol.
How to calculate Maximum Rate given Modifying Factor in Michaelis Menten Equation using this online calculator? To use this online calculator for Maximum Rate given Modifying Factor in Michaelis Menten Equation, enter Initial Reaction Rate (V0), Enzyme Modifying Factor (α), Michaelis Constant (KM), Enzyme Substrate Modifying Factor (α') & Substrate Concentration (S) and hit the calculate button. Here is how the Maximum Rate given Modifying Factor in Michaelis Menten Equation calculation can be explained with given input values -> 0.0054 = (450*((5*3000)+(2*1500)))/1500.