Question 1

What caused a "burst" of activity followed by a steady-state reaction when chymotrypsin was studied by stop-flow techniques?

Accepted Answer

The answer of What caused a "burst" of activity followed...

Question 2

The metal most commonly found at the active site of metalloproteases is:

Accepted Answer

A)  zinc. 
B)  calcium. 
C)  selenium. 
D)  magnesium. 
E)  sodium.

Question 3

A ________________ catalytic mechanism that forces two substrates into an appropriate three-dimensional arrangement for the reaction to occur.

Accepted Answer

The answer of A ________________ catalytic mechanism that forces two...

Question 4

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The type of catalysis in which two substrates are brought into close proximity.

Accepted Answer

A) hydrolysis 
B) affinity label 
C) tyrosinase 
D) chymotrypsin 
E) pepsin
F)noncompetitive
G)uncompetitive
H)heterotropic
I)approximation and orientation
J)acid-base
K)competitive

Question 5

There is a key difference between an enzyme that uses a covalent catalysis mechanism and one that uses other catalytic strategies. What is this key difference?

Accepted Answer

The answer of There is a key difference between an...

Question 6

An uncompetitive inhibitor will have two ________________ lines on a double-reciprocal plot.

Accepted Answer

The answer of An uncompetitive inhibitor will have two ________________...

Question 7

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: An enzyme that is part of a pigment formation pathway and has a low optimum temperature.

Accepted Answer

A) hydrolysis 
B) affinity label 
C) tyrosinase 
D) chymotrypsin 
E) pepsin
F)noncompetitive
G)uncompetitive
H)heterotropic
I)approximation and orientation
J)acid-base
K)competitive

Question 8

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: A type of enzyme inhibitor where KM is unaltered.

Accepted Answer

A) hydrolysis 
B) affinity label 
C) tyrosinase 
D) chymotrypsin 
E) pepsin
F)noncompetitive
G)uncompetitive
H)heterotropic
I)approximation and orientation
J)acid-base
K)competitive

Question 9

What are group-specific reagents?

Accepted Answer

The answer of What are group-specific reagents?...

Question 10

Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage?

Accepted Answer

A)  his, ser, asp 
B)  his, ser 
C)  asp, lys 
D)  lys, arg 
E)  his, ser, arg

Question 11

The ________________ stabilizes the tetrahedral intermediate of the hydrolysis of a peptide bond by chymotrypsin.

Accepted Answer

The answer of The ________________ stabilizes the tetrahedral intermediate of...

Question 12

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: An enzyme that temporarily undergoes covalent catalysis as part of its mechanism.

Accepted Answer

A) hydrolysis 
B) affinity label 
C) tyrosinase 
D) chymotrypsin 
E) pepsin
F)noncompetitive
G)uncompetitive
H)heterotropic
I)approximation and orientation
J)acid-base
K)competitive

Question 13

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The enzyme inhibition that can be overcome by increasing the concentration of substrate.

Accepted Answer

A) hydrolysis 
B) affinity label 
C) tyrosinase 
D) chymotrypsin 
E) pepsin
F)noncompetitive
G)uncompetitive
H)heterotropic
I)approximation and orientation
J)acid-base
K)competitive

Question 14

How is specificity determined by chymotrypsin?

Accepted Answer

A)  by an interaction of the active site amino acids with the substrate 
B)  by a binding of the N-terminus amino acid at the active site 
C)  by a covalent binding of a his residue to the substrate 
D)  by a conformational change upon the binding of substrate 
E)  by a binding of the proper amino acid into a deep pocket on the enzyme

Question 15

How is the enzyme chymotrypsin bind and hydrolyze its substrate? How does this differ from other proteases?

Accepted Answer

The answer of How is the enzyme chymotrypsin bind and...

Question 16

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The inhibitor which binds only to the ES complex and lowers the Vmax and KM.

Accepted Answer

A) hydrolysis 
B) affinity label 
C) tyrosinase 
D) chymotrypsin 
E) pepsin
F)noncompetitive
G)uncompetitive
H)heterotropic
I)approximation and orientation
J)acid-base
K)competitive

Question 17

Designing drugs to inhibit enzymes is a large part of pharmaceutical research. What are some of the enzymatic features that would be important?

Accepted Answer

The answer of Designing drugs to inhibit enzymes is a...

Question 18

What factors should an enzymologist consider when designing an enzyme assay?

Accepted Answer

The answer of What factors should an enzymologist consider when...

Question 19

Bacteria that become penicillin resistant express an enzyme called β-lactamase. This enzyme hydrolyses the lactam ring on penicillin. Suggest a reason why this protein allows cells to grow in the presence of penicillin.

Accepted Answer

The answer of Bacteria that become penicillin resistant express an...

Question 20

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The type of reaction catalyzed by proteases.

Accepted Answer

A) hydrolysis 
B) affinity label 
C) tyrosinase 
D) chymotrypsin 
E) pepsin
F)noncompetitive
G)uncompetitive
H)heterotropic
I)approximation and orientation
J)acid-base
K)competitive

Exam 8: Mechanisms and Inhibitors

What caused a "burst" of activity followed by a steady-state reaction when chymotrypsin was studied by stop-flow techniques?

The metal most commonly found at the active site of metalloproteases is:

A ________________ catalytic mechanism that forces two substrates into an appropriate three-dimensional arrangement for the reaction to occur.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: The type of catalysis in which two substrates are brought into close proximity.

There is a key difference between an enzyme that uses a covalent catalysis mechanism and one that uses other catalytic strategies. What is this key difference?

An uncompetitive inhibitor will have two ________________ lines on a double-reciprocal plot.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: An enzyme that is part of a pigment formation pathway and has a low optimum temperature.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: A type of enzyme inhibitor where KM is unaltered.

What are group-specific reagents?

Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage?

The ________________ stabilizes the tetrahedral intermediate of the hydrolysis of a peptide bond by chymotrypsin.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: An enzyme that temporarily undergoes covalent catalysis as part of its mechanism.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: The enzyme inhibition that can be overcome by increasing the concentration of substrate.

How is specificity determined by chymotrypsin?

How is the enzyme chymotrypsin bind and hydrolyze its substrate? How does this differ from other proteases?

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: The inhibitor which binds only to the ES complex and lowers the Vmax and KM.

Designing drugs to inhibit enzymes is a large part of pharmaceutical research. What are some of the enzymatic features that would be important?

What factors should an enzymologist consider when designing an enzyme assay?

Bacteria that become penicillin resistant express an enzyme called β-lactamase. This enzyme hydrolyses the lactam ring on penicillin. Suggest a reason why this protein allows cells to grow in the presence of penicillin.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: The type of reaction catalyzed by proteases.