Biochemistry
Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 6, Problem 1RE

RECALL How does the catalytic effectiveness of enzymes compare with that of nonenzymatic catalysts?

Expert Solution & Answer
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Interpretation Introduction

Interpretation:

The comparison between the catalytic effectiveness of the enzyme and the nonenzymatic catalysts.

Concept introduction:

The process through which the rate of a chemical reaction is increased is termed as catalysis. The functional proteins and some self-splicing ribonucleic acid molecules serve to increase the rate of a reaction and they are known as catalysts. In the biological system, they are known as enzymes.

Enzymes are largely organic in nature and are produced by the organism’s body itself, while catalysts can be organic or inorganic in nature. The catalysts and enzymes are not used up in the chemical reaction, they just alter the rate of the reaction.

Answer to Problem 1RE

The enzymatic catalysts are mainly proteins and some RNA molecules that show higher catalytic activity in terms of specificity, the speed of the reaction than nonenzymatic catalysts, which are organic or inorganic molecules.

Explanation of Solution

The difference between the enzymatic catalysts and nonenzymatic catalysts are as follows:

Enzymatic catalyst Nonenzymatic catalyst
The enzymatic catalysts are complex proteins and speed up the chemical reactions that occur in the biological system. The nonenzymatic catalyst increases or decreases the rate of chemical reactions that occur outside the biological system.
The enzymatic catalysts are highly specific in nature. The nonenzymatic catalysts are not very specific in nature.
The enzymatic catalysts increase the rate of reaction by an order of 1020. The nonenzymatic catalysts are comparatively slower and increase the rate of reaction about 102 to 104 times.
The enzyme catalyst requires optimum physiological conditions. The nonenzymatic catalysts require high temperature or pressure.
Conclusion

Therefore, it can be concluded that the catalytic effectiveness of the enzymatic catalyst is higher than that of a nonenzymatic catalyst. The enzymatic catalyst is more specific in nature than the nonenzymatic catalyst.

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Chapter 6 Solutions

Biochemistry

Ch. 6 - REFLECT AND APPLY An enzyme catalyzes the...Ch. 6 - REFLECT AND APPLY Can the presence of a catalyst...Ch. 6 - RECALL For the hypothetical reaction 3A+2B2C+3D...Ch. 6 - REFLECT AND APPLY The enzyme lactate dehydrogenase...Ch. 6 - REFLECT AND APPLY Would you use a pH meter to...Ch. 6 - REFLECT AND APPLY Suggest a reason for carrying...Ch. 6 - RECALL Distinguish between the lock-and-key and...Ch. 6 - RECALL Using an energy diagram, show why the...Ch. 6 - REFLECT AND APPLY Other things being equal, what...Ch. 6 - REFLECT AND APPLY Amino acids that are far apart...Ch. 6 - REFLECT AND APPLY If only a few of the amino acid...Ch. 6 - RECALL Show graphically how the reaction velocity...Ch. 6 - RECALL Define steady state, and comment on the...Ch. 6 - RECALL How is the turnover number of an enzyme...Ch. 6 - MATHEMATICAL For an enzyme that displays...Ch. 6 - MATHEMATICAL Determine the values of KM and Vmax...Ch. 6 - MATHEMATICAL The kinetic data in the following...Ch. 6 - MATHEMATICAL The enzyme -methylaspartase catalyzes...Ch. 6 - MATHEMATICAL The hydrolysis of a...Ch. 6 - MATHEMATICAL For the Vmax obtained in Question 26,...Ch. 6 - MATHEMATICAL You do an enzyme kinetic experiment...Ch. 6 - REFLECT AND APPLY The enzyme D-amino acid oxidase...Ch. 6 - REFLECT AND APPLY Why is it useful to plot rate...Ch. 6 - REFLECT AND APPLY Under what conditions can we...Ch. 6 - BIOCHEMICAL CONNECTIONS Why does acetazolamide...Ch. 6 - BIOCHEMICAL CONNECTIONS How did scientists...Ch. 6 - BIOCHEMICAL CONNECTIONS How do the KM values for...Ch. 6 - Prob. 38RECh. 6 - RECALL What are the three most common mechanisms...Ch. 6 - RECALL What is the biggest difference between a...Ch. 6 - RECALL How do scientists determine the KM of a...Ch. 6 - Prob. 42RECh. 6 - Prob. 43RECh. 6 - RECALL Do all enzymes display kinetics that obey...Ch. 6 - RECALL How can you recognize an enzyme that does...Ch. 6 - RECALL If we describe an enzyme like aspartate...Ch. 6 - RECALL How can competitive and pure noncompetitive...Ch. 6 - RECALL Why does a competitive inhibitor not change...Ch. 6 - RECALL Why does a pure noncompetitive inhibitor...Ch. 6 - RECALL Distinguish between the molecular...Ch. 6 - RECALL Can enzyme inhibition be reversed in all...Ch. 6 - RECALL Why is a Lineweaver-Burk plot useful in...Ch. 6 - RECALL Where do lines intersect on a...Ch. 6 - RECALL What is the difference between pure and...Ch. 6 - REFLECT AND APPLY Why can we say that having a...Ch. 6 - REFLECT AND APPLY When we compare the binding of I...Ch. 6 - RECALL Why does the apparent KM decrease in the...Ch. 6 - RECALL What is a suicide substrate? Why are they...Ch. 6 - RECALL If we made a Lineweaver-Burk plot of an...Ch. 6 - Prob. 60RECh. 6 - MATHEMATICAL For the following aspartase reaction...Ch. 6 - REFLECT AND APPLY Is it good (or bad) that enzymes...Ch. 6 - REFLECT AND APPLY Noncompetitive inhibition is a...Ch. 6 - BIOCHEMICAL CONNECTIONS You have been hired by a...Ch. 6 - REFLECT AND APPLY Would you expect an irreversible...Ch. 6 - REFLECT AND APPLY Would you expect the structure...Ch. 6 - Prob. 67RECh. 6 - Prob. 68RE
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