BIOCHEMISTRY
ENZYMES AND METABOLISM
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Question
[CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
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To calculate the free energy
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Mathematically explain the relationship of enzyme’s velocity and the substrate concentration
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Mathematically explain the saturation of enzyme in substrate
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To simplify Lineweaver-Burke plot
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Detailed explanation-1: -The Michaelis-Menten equation for this system is: Here, Vmax represents the maximum velocity achieved by the system, at maximum (saturating) substrate concentrations. KM (the Michaelis constant; sometimes represented as KS instead) is the substrate concentration at which the reaction velocity is 50% of the Vmax.
Detailed explanation-2: -The Michaelis-Menten equation can then be rewritten as V= Kcat [Enzyme] [S] / (Km + [S]). Kcat is equal to K2, and it measures the number of substrate molecules “turned over” by enzyme per second. The unit of Kcat is in 1/sec.
Detailed explanation-3: -The Michaelis–Menten equation is mainly used to characterize the enzymatic rate at different substrate concentrations, but it is also widely applied to characterize the elimination of chemical (the first-order kinetics) compounds from the body.
Detailed explanation-4: -For an enzyme-catalysed reaction, there is usually a hyperbolic relationship between the rate of reaction and the concentration of substrate, as shown below: (A) At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration.
Detailed explanation-5: -The Michaelis-Menten equation has been widely used for over a century to estimate the enzyme kinetic parameters from reaction progress curves of substrates, which is known as the progress curve assay.