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 Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant?
Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant calculator uses Apparent Michaelis Constant = Michaelis Constant*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant)) to calculate the Apparent Michaelis Constant, The Apparent Michaelis Menten constant given inhibitor's dissociation constant formula is defined as the relation with inhibitor's dissociation constant and with the inhibitor concentration. Apparent Michaelis Constant is denoted by Kmapp symbol.
How to calculate Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant using this online calculator? To use this online calculator for Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant, enter Michaelis Constant (KM), Inhibitor Concentration (I) & Enzyme Inhibitor Dissociation Constant (Ki) and hit the calculate button. Here is how the Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant calculation can be explained with given input values -> 0.004421 = 3000*(1+(9000/19000)).