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Chapter 16: Q. 16.77 (page 581)

How would the lock-and-key model explain that sucrase hydrolyzes sucrose, but not lactose?

Short Answer

Expert verified

Sucrose conducts catalyzed since this fits the form of the active site in sucrase, however lactose doesn't quite.

Step by step solution

01

Introduction

According to lock and key theory, a precursor complements the active site's design and makes an enzyme called that facilitates the activity.

02

Given Information

The substrate will also not be activated if something doesn't flow inside of the catalytic.

03

Explanation

Sucrose conducts catalyzed since this fits the form of the active site in sucrase, however lactose doesn't quite even though it does not engage in the catalytic site of serum protein.

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Most popular questions from this chapter

Indicate whether each of the following would be a substrate(S)or an enzyme (E):(16.4)

a.lactose

b.lipase

c.amylase

d.trypsin

e.pyruvate

f.transaminase

Aspartame, which is used in artificial sweeteners, contains the following dipeptide:

a. What are the amino acids in aspartame?

b. How would you name the dipeptide in aspartame?

How does the polarity of the R group in leucine compare to the R group in serine?

What is the reactant for each of the following enzymes?

a. peptidase

b. cellulase

c. lactase

Indicate whether each of the following describes a competitive or a noncompetitive enzyme inhibitor:

a. The inhibitor has a structure similar to the substrate.

b. The effect of the inhibitor cannot be reversed by adding more substrate.

c. The inhibitor competes with the substrate for the active site,

d. The structure of the inhibitor is not similar to the substrate.

e. The addition of more substrate reverses the inhibition.
See all solutions

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