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Chapter 12: Q4. (page 373)

Derive the Michaelis鈥揗enten equation.

Short Answer

Expert verified

The Michaelis-Menten equation isv=VmaxSS+KM.

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=VmaxSS+KM

Where,

V= Velocity of the reaction

Vmax= Maximum velocity of the reaction

[S]= Substrate concentration

KM= Michaelis constant

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Most popular questions from this chapter

You are attempting to determine KM by measuring the reaction velocity at different substrate concentrations, but you do not realize thatthe substrate tends to precipitate under the experimental conditions youhave chosen. How would this affect your measurement of KM?

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?

How does pure non-competitive inhibition differ from other forms of inhibition?

For an enzymatic reaction, draw curves that show the appropriate relationships between the variables in each plot below.

Why are uncompetitive and mixed inhibitors generally considered to be more effective in vivo than competitive inhibitors?
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