Amino Acids, Proteins, and Enzymes

An Introduction to General, Organic, and Biological Chemistry ยท 85 exercises

Q. 16.50

In humans, the antihiotic amoxicillin (a type of penicillin) is used to treat certain bacterial infections.

a. Docs the antibiotic inhibit emzymes in humans?

b. Why does the antabiotic kill bacteria, but not humans?

c. Is anosicillin a reversible or irreversible inhabitor?

7 step solution

Q. 16.51

What is the chemical formula for hydroxyurea?

3 step solution

Q. 16.54

Fetal hemoglobin binds oxygen more tightly than does adult hemoglobin. Why do you think fetal hemoglobin functions differently than adult hemoglobin?

3 step solution

Q. 16.49

Methanol and ethanol are oxidized by alcohol dehydrogenase. In methanol poisoning, ethanol is given intravenously to prevent the formation of formaldehyde that has toxic effects.

a. Draw the condensed structural formulas for methanol and ethanol.

b. Would ethanol compete for the active site or bind to a different site?

c. Would ethanol be a competitive or noncompetitive inhibitor of alcohol dehydrogenase?

7 step solution

Q. 16.52

What is the molar mass of hydroxyurea?

4 step solution

Q.16.55

Ethylene glycol HOCH2CH2OH is a major component of antifreeze. If ingested, it is first converted to HOOC-CHO oxoethanoic acid and then to HOOC-COOH oxalic acid, which is toxic added to a radiator to prevent freezing and boiling.

a. What class of enzyme catalyzes the reactions described?

b. The treatment for the ingestion of ethylene glycol is an intravenous solution of ethanol. How might this help prevent toxic levels of oxalic acid in the body?

4 step solution

Q. 16.56

Adults who are lactose intolerant cannot break down the disaccharide in milk products. To help digest dairy food, a product known as Lactaid can be added to milk and the milk then refrigerated for 24 hours?


a. What enzyme is present in Lactaid, and what is the major class of this enzyme?

b. What might happen to the enzyme if the Lactaid were stored at 55C ?

5 step solution

Q.16.60

What type of interaction would you expect between the following in a tertiary structure?

a. threonine and glutamine

b. valine and alanine

c. arginine and glutamate

6 step solution

Q.16.66

What are some differences between each of the following pairs? 

a. a salt bridge and a disulfide bond

b. an α helix and collagen

c. α helix and β-pleated sheet

d. tertiary and quaternary structures of proteins

8 step solution

Q. 16.57

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?

5 step solution

Q. 16.63

Seeds and vegetables are often deficient in one or more essential amino acids. Using the following table, state whether each combination provides all of the essential amino acids: 


a. rice and garbanzo beans.

b. lima beans and cornmeal.

c. garbanzo beans and lima beans.

7 step solution

Q. 16.58

Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins.


a.  The directions for a gelatin (protein) dessert say not to add fresh pineapple. However, canned pineapple where                   pineapple is heated to high temperatures can be added. Why?

b.  Fresh pineapple is used in a marinade to tenderize tough meat. Why?

c.  What structural level of a protein does the bromelain enzyme destroy?

6 step solution

Q. 16.64

Seeds and vegetables are often deficient in one or more essential amino acids. Using the table in problem, state whether each combination provides all of the essential amino acids. 


a. rice and lima beans.

b. rice and oatmeal.

c. oatmeal and lima beans.

7 step solution

Q. 16.59

Identify the amino acids and type of interaction that occurs between the following  R groups in tertiary protein structures:


a)

                   


b)

             


c)

               


d)

                  

9 step solution

Q. 16.61

a. Draw the condensed structural formula for Ser-Lys-Asp. 

b. Would you expect to find this segment at the center or at the surface of a protein? Why?

4 step solution

Q. 16.62

a. Draw the condensed structural formula for Val-Ala-Leu. 

b. Would you expect to find this segment at the center or at the surface of a protein? Why?

4 step solution

Q. 16.65

What are sonse differences between each of the following pairs? (16.1, 16.2. 16.3)

a. secondary and tertiary protein structures

b. exsential and nonessential amino acids

c. polar and nonpolar amino acids

d. dipeptides and tripeptides

9 step solution

Q.16.73

Indicate whether ench 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

15 step solution

Q. 16.73

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

3 step solution

Q. 16.73

 Indicate whether eachof 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

3 step solution

Q. 16.67

If glutamate were replaced by proline in a protein, how might the tertiary structure be affected? (16.1, 16.3)

4 step solution

Q. 16.68

If glycine were replaced by alanine in a protein, how might the tertiary structure be affected? (16.1,16.3)

4 step solution

Q. 16.69

How do enzymes differ from catalysts used in chemical laboratories? (16.4)

2 step solution

Q. 16.7

Why do enzymes function only under mild conditions? (16.4,16.5)

2 step solution

Q. 16.79

If a blood test indicates a high level of LDH and CK, what could be the cause?

3 step solution

Q. 16.80

If a blood test indicates a high level of ALT, what could be the cause? 

3 step solution

Q. 16.81

Consider the amino acids lysine, valine, and aspartate in an enzyme. State which of these amino acids have R groups that would:

a. be found in hydrophobic regions.

b. be found in hydrophilic regions.

c. form hydrogen bonds.

d. form salt bridges.

9 step solution

Q. 16.77

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

3 step solution

Q. 16.78

16.78 How does the induced-fit model of enzyme action allow an enzyme to catalyze a reaction of a group of substrates? 

3 step solution

Q. 16.82

Consider the amino acids histidine, phenylalanine, and serine in an enzyme. State which of these amino acids have R groups that would:

a. be found in hydrophobic regions

b. be found in hydrophilic regions

c. form hydrogen bonds

d. form salt bridges

9 step solution

Q. 16.72

16.72 Maltase is an enzyme that hydrolyzes maltose to two glucose molecules. (16.4)

a. What are the reactants and products of the reaction?

b. Draw an energy diagram for the reaction with and without maltase.

c. How does maltase make the reaction go faster?

7 step solution

Q. 16.74

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

a. glucose

b. hydrolase

c. maleate isomerase

d. alanine

e. amylose

f. lactase

13 step solution

Q. 16.71

Lactase is an enzyme that hydrolyzes lactose to glucose and galactose.

a. What are the reactants and products of the reaction?

b. Draw an energy diagram for the reaction with and without lactase.

c. How does lactase make the reaction go faster?

7 step solution

Q. 16.75

Give the substrate of each of the following enzymes: (16.4)

a. urease

b. succinate dehydrogenase

c. aspartate transaminase

d. tyrosinase

6 step solution

Q. 16.76

Give the substrate of each of the following enzymes: (16.4)

a. maltase

b. fructose oxidase

c. phenolase

d. sucrase(16.4)

9 step solution

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