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Chapter 12: Q24P (page 399)

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?

Short Answer

Expert verified

The experimentally determined KM will be very high than the calculated one.

Step by step solution

01

Enzymes

Enzymes are biological protein catalysts that change the rate of a process in a living organism. The molecule that binds to the enzyme's substrate binding site is referred to as the substrate.

02

Measurement of KMaffected when the substrate tends to precipitate

The substrate concentration will be lower if the substrate forms a precipitate under the experimental conditions. There won't be enough substrate to bind to the enzyme because there won't be enough of it. The reaction's velocity is affected as a result of this. As a result, the calculated KMwill be significantly higher than the experimentally determined one.

KM measurement will be affected when the substrate starts to precipitate.

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Most popular questions from this chapter

Enzyme Acatalyzes the reactions S to P and has a KM of 50μMand a Vmaxof 100nMs‐1. Enzyme Bcatalyzes the reaction S→Q and has a KM of 5mMand a Vmax of 120nMs‐1. When 100μM of S is added to a mixture containing equivalent amounts of enzymes A andB , after 1minute which reaction product will be more abundant: P or Q?

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*)if the reaction follows a Ping Pong mechanism?

Describe the effects of competitive, uncompetitive, and mixed inhibitors on KM and Vmax.

For the same enzyme sample described in Problem 27, what would your results show if a reversible inhibitor is present?

Explain the structural basis for cooperative substrate binding and allosteric control in ATCase.
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