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Biochemistry Module Exam 3 | LATEST UPDATED | 53 COMPLETE QUESTIONS AND ANSWERS | 100% RATED CORRECT | ALREADY GRADED A+

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Biochemistry Module Exam 3 | LATEST UPDATED | 53 COMPLETE QUESTIONS AND ANSWERS | 100% RATED CORRECT | ALREADY GRADED A+

Institution
Biochemistry Module
Course
Biochemistry Module

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Biochemistry Module Exam 3 | 2025-2026 LATEST UPDATED | 53

COMPLETE QUESTIONS AND ANSWERS | 100% RATED CORRECT |

ALREADY GRADED A+

Which of the following statements about enzymes are true:


1. Catalysis occurs at the active site, which usually consists of a crevice on the surface of the
enzyme.
2. Generally, an enzyme is specific for a particular substrate. For example, thrombin catalyzes
the hydrolysis of the peptide bond between Arg and Gly.
3. An enzyme yields a specific product, whereas a nonbiological catalyst may produce more than
one product, and side reactions may occur.

4. Nonbiological catalysts and enzymes tend to have a similar degree of reaction specificity.
5. A substrate must bind to the active site before catalysis can occur. - (answers)1,2,3,5



general enzyme-catalyzed reaction. - (answers)E + S ↔ ES ↔ E + P



What effects are produced by an enzyme on the general reaction below



S↔P
k1→

k2←

2. the activation energy for the reaction is lowered.

3. the rate constant for the reverse reaction (k2) increases.

4. ∆G for the reaction decreases.

5. The formation of the transition state is promoted.

6.The concentration of the products is increased. - (answers)2,3,5


心也是善良与爱的源泉。

,Which of the following interactions can contribute to the intrinsic binding energy during
enzymatic catalysis:



1. permanent covalent bonding

2. electrostatic interactions

3. nucleophilic attack by serine

4. hydrogen bonding
5. van der waals interactions - (answers)2, 4, 5


sort the following into: acid-base catalysis, covalent catalysis, metal ion catalysis, or all.



1. catalyst retains its original form after reaction occurs.

2. a proton is transferred between enzyme and substrate.

3. a covalent bond forms between enzyme and substrate.
4. may use amino acids such as aspartate or lysine for protonation or proton abstraction.

5. may take part in interactions involving Fe2+.

6. Catalysts may participate in oxidation-reduction reactions by changes in the oxidation state.

7. uses a nucleophilic function group.

8. lowers the energy or stabilizes the transition state or intermediate.

9. a Zn2+ cofactor may properly orient the substrate in the active site through ionic interactions.

10. two-part catalytic process(for example, the chymotrypsin mechanism). - (answers)acid-base
catalysis: 2, 4



covalent catalysis: 3, 7, 10


metal ion catalysis: 5,6,9



all: 8, 1
心也是善良与爱的源泉。

, suppose that an arginine residue in the active site of an enzyme was mutated to alanine. as
expected, the alanine mutant was inactive, suggesting that the arginine residue was critical to the
catalytic mechanism.

which mutantion is most likely to restore wild-type level of activity to the alanine mutant.



a to e

a to k

a to m
a to y

a to s - (answers)A TO K



sort the following into lock-and-key model, induced-fit model, or common to both.



1. substrate binds to the enyzme at the active site, forming an enzyme-substrate complex.

2.enzyme active site has a rigid structure complementary to that of the substrate.
3.substrate binds to the enzyme through noncovalent interactions.

4. enzyme conformation changes when it binds the substrate so the active site fits the substrate. -
(answers)lock-and-key model: 2


induced-fit model: 4



common to both: 1, 3



which statements are true:

1. one HIS residue abstracts a proton from the substrate at pH 6.0 whereas the other donates a
proton.

2. The RNAse reaction is an example of metal ion catalysis with a positvely charged metal.

心也是善良与爱的源泉。

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