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Chapter 12: Q4. (page 373)

Derive the Michaelis–Menten equation.

Short Answer

Expert verified

The Michaelis-Menten equation is $v = V_{max} (\frac{[S]}{[S] {+K}_{M}})$ .

Step by step solution

01

Michaelis-Menten equation

By connecting the rate of reaction (product production) to the substrate concentration, the Michaelis-Menten equation determines the rate of enzyme catalysis. The equation is:

$v = V_{max} (\frac{[S]}{[S] {+K}_{M}})$

Where,

V= Velocity of the reaction

V_max= Maximum velocity of the reaction

[S]= Substrate concentration

K_M= Michaelis constant

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Most popular questions from this chapter

Why are such allosteric enzymes composed of more than one catalytic subunit?

At what concentration of $S$ (expressed as a multiple of $K_{M}$ ) will $v_{0} = 0.95 V_{\max}$ ?

List the factors that influence a drug’s bioavailability.

In a bisubstrate reaction, a small amount of the first product P is isotopically labeled (P*) and added to the enzyme and the first substrate A. No B or Q is present. Will A (=P-X) become isotopically labeled (A*) ifthe reaction follows a Sequential mechanism?

Summarize the purpose of phases I through III of a clinical trial.

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