
One of the ways biochemists characterize enzymes is to study the rates of enzymecatalyzed reactions, a field known as enzyme kinetics. The study of enzyme kinetics provides researchers with clues as to how enzymes work. In 1913, Leonor Michaelis and Maud Menten derived a rate law that governs enzyme kinetics. 
MichaelisMenten enzyme kinetics can be modeled by the following equation,
where V represents the reaction velocity, V_{max} represents the maximum reaction velocity, K_{m }represents the MichaelisMenten constant, and [S] represents the substrate concentration.
Note of caution
This equation assumes that during the reaction the concentration of the enzymesubstrate complex remains constant and is lower than the concentrations of unbound substrate. These conditions are known as steadystate. 
Looking at the equation, one can readily see that the velocity of the reaction, V , is dependent on the substrate concentration,
[S]. In fact, the MichaelisMenten equation is a rational function. As rational functions can be difficult to work with graphically, the
MichaelisMenten equation can be transformed into a linear equation by taking
the reciprocal of both sides as,
This new equation is called the LineweaverBurk equation after the researchers who derived it in 1934. The LineweaverBurk equation is a linear equation, where 1/V is a linear function of 1/[S]
instead of V being a rational function of [S]. The LineweaverBurk equation
can be readily represented graphically to determine the values of K_{m} and V_{max}.
Now use the LineweaverBurk equation to answer the following questions:
Determine the slope of the line represented by the LineweaverBurk equation.
Determine the 1/V intercept of the LineweaverBurk equation.
Given a LineweaverBurk plot, determine the V_{max} of a particular enzyme.
Given a LineweaverBurk plot, determine the K_{m} of a particular enzyme.
Determine the 1/[S]intercept of the LineweaverBurk equation.
Compare a LineweaverBurk plot to a MichaelisMenten plot for the same data set.
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