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 Inhibitor's Dissociation Constant given Michaelis Menten Constant?
Inhibitor's Dissociation Constant given Michaelis Menten Constant calculator uses Enzyme Inhibitor Dissociation Constant = (Inhibitor Concentration/((Apparent Michaelis Constant/Michaelis Constant)-1)) to calculate the Enzyme Inhibitor Dissociation Constant, The Inhibitor's dissociation constant given Michaelis Menten constant formula is defined as the relation with Michaelis constant and apparent Michaelis constant and with the inhibitor concentration. Enzyme Inhibitor Dissociation Constant is denoted by Ki symbol.
How to calculate Inhibitor's Dissociation Constant given Michaelis Menten Constant using this online calculator? To use this online calculator for Inhibitor's Dissociation Constant given Michaelis Menten Constant, enter Inhibitor Concentration (I), Apparent Michaelis Constant (Kmapp) & Michaelis Constant (KM) and hit the calculate button. Here is how the Inhibitor's Dissociation Constant given Michaelis Menten Constant calculation can be explained with given input values -> 0.003 = (9000/((12000/3000)-1)).