Apparent Maximum Rate in Enzyme Kinetics Formulas

Apparent Maximum Rate is defined as the maximum speed achieved by the system at saturated substrate concentration in presence of non-competitive inhibitor. And is denoted by Vmax^app. Apparent Maximum Rate is usually measured using the Mole per Liter Second for Reaction Rate. Note that the value of Apparent Maximum Rate is always negative.

Formulas to find Apparent Maximum Rate in Enzyme Kinetics

fxApparent Maximum Rate in presence of Noncompetitive InhibitorGo

Enzyme Kinetics formulas that make use of Apparent Maximum Rate

fxDissociation Constant in presence of Noncompetitive InhibitorGo

fxMaximum Rate in presence of Noncompetitive InhibitorGo

fxInhibitor Concentration in presence of Noncompetitive InhibitorGo

List of variables in Enzyme Kinetics formulas

fx Maximum Rate Go

fx Inhibitor Concentration Go

fx Enzyme Inhibitor Dissociation Constant Go

FAQ

What is the Apparent Maximum Rate?

Apparent Maximum Rate is defined as the maximum speed achieved by the system at saturated substrate concentration in presence of non-competitive inhibitor. Apparent Maximum Rate is usually measured using the Mole per Liter Second for Reaction Rate. Note that the value of Apparent Maximum Rate is always negative.

Can the Apparent Maximum Rate be negative?

Yes, the Apparent Maximum Rate, measured in Reaction Rate can be negative.

What unit is used to measure Apparent Maximum Rate?

Apparent Maximum Rate is usually measured using the Mole per Liter Second[mol/L*s] for Reaction Rate. Millimole per Liter Second[mol/L*s], Mole per Cubic Meter Second[mol/L*s] are the few other units in which Apparent Maximum Rate can be measured.

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