Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant Solution

STEP 0: Pre-Calculation Summary
Formula Used
Apparent Michaelis Constant = Michaelis Constant*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant))
Kmapp = KM*(1+(I/Ki))
This formula uses 4 Variables
Variables Used
Apparent Michaelis Constant - (Measured in Mole per Cubic Meter) - The Apparent Michaelis Constant is defined as the Michaelis–Menten constant in the presence of a competitive inhibitor.
Michaelis Constant - (Measured in Mole per Cubic Meter) - The Michaelis Constant is numerically equal to the substrate concentration at which the reaction rate is half of the maximum rate of the system.
Inhibitor Concentration - (Measured in Mole per Cubic Meter) - The Inhibitor concentration is defined as the number of moles of inhibitor present per liter of solution of the system.
Enzyme Inhibitor Dissociation Constant - (Measured in Mole per Cubic Meter) - The Enzyme Inhibitor Dissociation Constant is measured by the method in which the inhibitor is titrated into a solution of enzyme and the heat released or absorbed is measured.
STEP 1: Convert Input(s) to Base Unit
Michaelis Constant: 3 Mole per Liter --> 3000 Mole per Cubic Meter (Check conversion here)
Inhibitor Concentration: 9 Mole per Liter --> 9000 Mole per Cubic Meter (Check conversion here)
Enzyme Inhibitor Dissociation Constant: 19 Mole per Liter --> 19000 Mole per Cubic Meter (Check conversion here)
STEP 2: Evaluate Formula
Substituting Input Values in Formula
Kmapp = KM*(1+(I/Ki)) --> 3000*(1+(9000/19000))
Evaluating ... ...
Kmapp = 4421.05263157895
STEP 3: Convert Result to Output's Unit
4421.05263157895 Mole per Cubic Meter -->4.42105263157895 Mole per Liter (Check conversion here)
FINAL ANSWER
4.42105263157895 4.421053 Mole per Liter <-- Apparent Michaelis Constant
(Calculation completed in 00.004 seconds)

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K J Somaiya College of science (K J Somaiya), Mumbai
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9 Noncompetitive Inhibitor Calculators

Dissociation Constant given Enzyme Substrate Complex Concentration
Go Enzyme Inhibitor Dissociation Constant = Inhibitor Concentration/(((((Initial Enzyme Concentration*Substrate Concentration)/Enzyme Substrate Complex Concentration)-Substrate Concentration)/Michaelis Constant)-1)
Apparent Initial Enzyme Concentration in Presence of Noncompetitive Inhibitor
Go Apparent Initial Enzyme Concentration = (Initial Enzyme Concentration/(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant)))
Initial Enzyme Concentration in presence of Noncompetitive Inhibitor
Go Initial Enzyme Concentration = (Apparent Initial Enzyme Concentration*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant)))
Dissociation Constant given Apparent Initial Enzyme Concentration
Go Enzyme Inhibitor Dissociation Constant = (Inhibitor Concentration/((Initial Enzyme Concentration/Apparent Initial Enzyme Concentration)-1))
Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant
Go Apparent Michaelis Constant = Michaelis Constant*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant))
Apparent Maximum Rate in presence of Noncompetitive Inhibitor
Go Apparent Maximum Rate = (Maximum Rate/(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant)))
Dissociation Constant in presence of Noncompetitive Inhibitor
Go Enzyme Inhibitor Dissociation Constant = (Inhibitor Concentration/((Maximum Rate/Apparent Maximum Rate)-1))
Maximum Rate in presence of Noncompetitive Inhibitor
Go Maximum Rate = (Apparent Maximum Rate*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant)))
Inhibitor Concentration in presence of Noncompetitive Inhibitor
Go Inhibitor Concentration = ((Maximum Rate/Apparent Maximum Rate)-1)*Enzyme Inhibitor Dissociation Constant

Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant Formula

Apparent Michaelis Constant = Michaelis Constant*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant))
Kmapp = KM*(1+(I/Ki))

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)).

FAQ

What is Apparent Michaelis Menten constant given Inhibitor's Dissociation 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 and is represented as Kmapp = KM*(1+(I/Ki)) or Apparent Michaelis Constant = Michaelis Constant*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant)). The Michaelis Constant is numerically equal to the substrate concentration at which the reaction rate is half of the maximum rate of the system, The Inhibitor concentration is defined as the number of moles of inhibitor present per liter of solution of the system & The Enzyme Inhibitor Dissociation Constant is measured by the method in which the inhibitor is titrated into a solution of enzyme and the heat released or absorbed is measured.
How to calculate Apparent Michaelis Menten constant given Inhibitor's Dissociation 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 is calculated using Apparent Michaelis Constant = Michaelis Constant*(1+(Inhibitor Concentration/Enzyme Inhibitor Dissociation Constant)). To calculate Apparent Michaelis Menten constant given Inhibitor's Dissociation Constant, you need Michaelis Constant (KM), Inhibitor Concentration (I) & Enzyme Inhibitor Dissociation Constant (Ki). With our tool, you need to enter the respective value for Michaelis Constant, Inhibitor Concentration & Enzyme Inhibitor Dissociation Constant and hit the calculate button. You can also select the units (if any) for Input(s) and the Output as well.
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