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 Modifying Factor of Enzyme Substrate Complex in Michaelis Menten Equation?
Modifying Factor of Enzyme Substrate Complex in Michaelis Menten Equation calculator uses Enzyme Substrate Modifying Factor = (((Maximum Rate*Substrate Concentration)/Initial Reaction Rate)-(Enzyme Modifying Factor*Michaelis Constant))/Substrate Concentration to calculate the Enzyme Substrate Modifying Factor, The Modifying factor of enzyme substrate complex in Michaelis Menten equation formula is defined as the enzyme activity under various substrate and inhibitor concentrations, to obtain a modified Michaelis–Menten equation. Enzyme Substrate Modifying Factor is denoted by α' symbol.
How to calculate Modifying Factor of Enzyme Substrate Complex in Michaelis Menten Equation using this online calculator? To use this online calculator for Modifying Factor of Enzyme Substrate Complex in Michaelis Menten Equation, enter Maximum Rate (Vmax), Substrate Concentration (S), Initial Reaction Rate (V0), Enzyme Modifying Factor (α) & Michaelis Constant (KM) and hit the calculate button. Here is how the Modifying Factor of Enzyme Substrate Complex in Michaelis Menten Equation calculation can be explained with given input values -> 78.88889 = (((40000*1500)/450)-(5*3000))/1500.