Chapter 20

Enzymes

Short Answer Questions

1. Name the six different classes of enzymes.

Answer: a) Oxido-reductases
b) Transferases
c) Hydrolases
d) Lyases
e) Isomerases
f) Ligases

2. To which class of enzymes would you assign an enzyme that carries out the
dehydrogenation of its substrate?
Answer: Oxido-reductases

3. To which class of enzymes does an enzyme belong if it catalyzes the rearrangement

of functional groups within a molecule?
Answer: Transferases

4. To which class of enzymes do lipases belong?

Answer: Hydrolases

5. How does an enzyme increase the rate of a chemical reaction?

Answer: By positioning substrates and destabilizing bonds and by
acting as organic catalysts . Enzyme increase the rate of reaction by
lowering the Energy of activation or (Ea). Enzyme achieve that by
attaching to the substrate in the active site and form the enzyme
substrate complex in-which the enzyme disturb the covalent bond of
the substrate causing it to enter the transitional state, which is the
most energetic and unstable state. The enzyme then breaks apart and
the substarte goes into an exorganic reaction and form the product.

6. The diagram below shows the energy pathway of an uncatalyzed reaction. Using the
same diagram, show the pathway of the same reaction when it is catalyzed by an
enzyme.
 Reactants

Products

Progress of reaction

Hint draw the figure and label it.

Answer:

Transitio
Activation
Energy
change
energy
n state
(∆
(E H) forthe
) for the
a
reaction
reaction

Free Reactants
Energy

Products

Reaction progress

7. For enzyme-catalyzed reactions, what happens as the concentration of the substrate

is increased?
Answer: The speed of chemical reaction also increases.
8. Why does the rate of an enzyme-catalyzed reaction not continue increasing
indefinitely as the concentration of substrate is increased?
Answer: As substrate concentration increases, the point is eventually
reached where enzymes capabilities are used to their maximum
extent. The rate remains constant from this point.

9. What is the first step in an enzyme-catalyzed reaction?

Answer: The first step involves formation of an enzyme-substrate
complex, E-S.

10. Name the portion of an enzyme that is in direct contact with the substrate.
Answer: Active site of enzymes

11. What type of specificity is exhibited by an enzyme that catalyzes the reaction of only
one substrate?
Answer: Absolute specificity

12. What adjective describes an enzyme that is able to catalyze a reaction of D-glucose,
but not L-glucose?
Answer: Stereochemical Specificity

13. The pancreatic enzymes trypsin, chymotrypsin, and elastase all hydrolyze peptide
bonds on the carbonyl side of several different amino acids in a protein. What is the term
for these enzymes which describes their specificity?
Answer: Carboxypeptidase

14. List three different ways in which an enzyme can affect the transition state in an
enzyme-catalyzed reaction.
Answer: Irreversible inhibitors, Reversible competitive inhibitors, and
Reversible noncompetitive inhibitors

15. What is the water-soluble vitamin from which NAD+ is made?

Answer: Vitamin B3 or niacin

16. What is the term for the pH at which an enzyme functions best?
Answer: Optimum pH range.

17. At extremes of pH an enzyme will lose its biologically active conformation. What
word describes the state of the enzyme under these conditions?
Answer: Transition state

18. What adjective describes an enzyme whose activity is regulated by the binding of a
small effector molecule?
Answer: Inhibitive

19. In feedback inhibition of an enzyme-catalyzed biosynthetic pathway, what substance

frequently serves as the negative allosteric effector?
Answer: Isoleucine
20. Proteolytic digestive enzymes are often produced in an inactive form. What is the
name of the inactive form of an enzyme?
Answer: Zymogens

21. What is the name of the zymogen form of pepsin?

Answer: Pepsinogen

22. Describe the binding between an irreversible inhibitor, such as arsenic, and an
enzyme.
Answer: Forms a strong covalent bond to an amino side chain group at
the inactive enzyme site.

23. Acetylcholine is a neurotransmitter that transmits a signal from a nerve cell to a

muscle cell, causing the muscle to contract. How is the neurotransmitter inactivated so
that the muscle can relax?
Answer: Inactivation can be through a reuptake mechanism or by an
enzyme that stops the action of the chemical.

24. Name the three products formed when acetylcholine undergoes hydrolysis,
catalyzed by acetylcholinesterase?
Answer: Choline, acetic acid

25. What is the term for an enzyme that hydrolyzes the bonds between amino acids in a
protein?
Answer: Proteases

26. What three pancreatic serine proteases have very similar primary and tertiary
structures?
Answer: Pepsin, Trypsin, and chymotrypsin

27. Chymotrypsin cleaves peptide bonds on the carbonyl side of what type of amino
acids?
Answer: Phenylalanine, Tryptophan, Tyrosine

28. Trypsin cleaves peptide bonds on the carbonyl side of what kind of amino acids?
Answer: Trypsin predominantly cleaves peptide chains at the carboxyl
side of the amino acids lysine or arginine, except when either is followed by
proline.

29. Elastase cleaves peptide bonds on the carbonyl side of which two amino acids?
Answer: Alanine and Valine

30. What are isoenzymes?

Answer: Isoenzymes are enzymes with the same function but slightly
different structural features.

31. How can appropriate analysis confirm that elevated levels of an enzyme such as
lactate dehydrogenase (LDH) in the blood are due to a recent heart attack and not
another disease?
 Answer: ( LHD 1 is found in the heart and red blood cells, while LDH-2
is concentrated in white blood cells.) Because LDH can be found in many
tissues in the body, total LDH is not specific for heart disease. Normally, the
level of LDH-2 is greater than LDH-1. However, after a heart attack, LDH-1
is generally higher than LDH-2. This is called a "flipped" LDH pattern. The
LDH level rises within 24 - 72 hours after a heart attack, peaks in 3 - 4 days,
and returns to normal in about 14 days.