Chapter 23

Enzyme and Catalyst Irreversible Inhibitor

Ribozymes Lyase
Substrate and Competitive Inhibitor Sulfa Drugs and p-Aminobenzoic Acid
Cofactor and Coenzyme Isomerase
-ase Le Chatelier’s Principle Ligase
Apoenzyme and Holoenzyme Allosterism and Allosteric Enzymes
Substrate and Active Site Active Site and Regulator Site
Enzyme-Substrate Complex Positive & Negative Modulation of
Enzyme Specificity and Activity Regulatory Enzyme Activity
Active Site Regulatory or Allosteric Enzymes
Transition State Regulator and Regulator Site
Transition State Analogs T and R Form of Allosteric Enzymes
Proenzyme and Zymogens Isozymes or Isoenzymes
Activation and Inhibition Proteases
Reversible and Irreversible Inhibition Immunogen
Competitive and Non-Competitive Catalytic Antibodies and Abzymes
Inhibitors Feedback Control of Enzyme Activity
Oxidoreductase Protein (Enzyme) Modification
pH Profile for Enzymatic Activity Kinases and Phosphatases
Transferase
Lock-and-Key and Induced-Fit Models
Hydrolase

1. A molecule that is structurally similar to the substrate for an enzyme will probably be a:
a. Competitive inhibitor
b. Cofactor
c. Regulator
d. Noncompetitive inhibitor
2. The site on an allosteric enzyme that is directly involved in modulation of its activity is
called
a. The prosthetic group
b. Regulatory site
c. Active site
d. Target site
3. The multistep sequence of reactions shown below uses a regulatory mechanism to control
the amount of D produced. In these general schemes, the last product, D, in the reaction
sequence is involved in a feed back mechanism of inhibiton. Molecule D in the sequence
usually
a. Inhibits E1
b. Inhibits E2
c. Inhibits E3
 d. Inhibits all enzymes

4. Competitive inhibition can be overcome by:

a. Increasing substrate concentration
b. Increasing pH
c. Decreasing temperature
d. All of above
5. Most enzymatic reactions are influenced by pH because pH changes can:
a. Completely hydrolyze the protein
b. Produce protonation or deprotonation of essential amino acid residues in the active
site
c. Change its primary structure
d. Effect the optical activity of the protein
6. A significant increase in the temperature (as when a patient has a very high fever) of an
enzymatic reaction may reduce the catalytic rate because the:
a. Enzyme acts on itself as an inhibitor
b. Protein is partially or completely denatured
c. Protein undergoes hydrolysis
d. Heat acts as a competitive inhibitor
7. Consider the possible shapes that a small molecule might have to act as a competitive
inhibitor to the reaction shown below:
Indicate which of the following molecules (molecular shape) could potentially act as a
competitive inhibitor

8. The apoprotein corresponds to which part of an enzyme?

a. Coenzyme
 b. Protein portion
c. Cofactor
d. Part cleaved off in a proenzyme
9. The site on the enzyme at which the substrate interacts is called the
a. Regulatory site
b. Modulator site
c. Active site
d. Allosteric site
10. A kinase is an enzyme that acts on another enzyme, A, to change its activity. A kinase
modifies enzyme A by
a. Cleaving enzyme A to produce a smaller active enzyme
b. Adding a missing coenzyme in the reaction
c. Adding a phosphate group on the enzyme
d. Adding a glycosyl group on the enzyme
11. Indicate which of the following characteristics an allosteric enzyme inhibits
a. A regulator molecule can bind strongly to the active site
b. The binding of a regulatory molecule to the regulatory site always inhibits
enzymatic activity
c. The binding of the regulatory molecule to the regulatory site can either increase or
decrease the enzymatic activity
d. The active site and the regulatory sites are always in different locations and cannot
be identical
e. In most cases, the allosteric enzyme s multi subunit protein
12. Characteristics of a proenzyme are:
a. They are made in the cell in an active form
b. They do not contain all the amino acid residues for a complete and active enzyme
c. Many proenzymes are usually cleaved (cut) to produce a smaller protein that
becomess the active enzyme
d. They do not have the correct prosthetic group for activity
13. The protein modification that is most common in the activiation of enzymes is:
a. Methylation
b. Phosphorylation
c. Addition of an aromatic group
d. Addition of an ester group
14. Allosteric regulator effector alters the activity of the enzyme:
a. It binds at the active site
b. It binds at the regulatory site
c. It can inhibit the enzyme activity
d. It can stimulate the enzyme activity

15. The small molecule, urea, is used to denature proteins. Its structure is
Its ability to denature proteins is primarily because
 a. It cleaves the peptide backbone
b. It breaks up essential hydrogen bonding in the secondary and tertiary structure
c. It breaks up hydrophobic interactions in the secondary and tertiary structure
d. It reacts with the hydroxyl group on glycine residues
16. Isoenzymes are enzymes that
a. Occur in different forms in different tissues and catalyze the same reaction
b. Are always composed of only one subunit
c. Must be modifies by a kinase to become active
d. Are unaffected by extreme temperatures
e. Are composed of RNA

Write the word, phrase or number in the blank space

1. Classify each of the following enzymes into one of the six major classes

Enzyme Classes

a. Acid phosphatase
a. Hydrolase
b. Alcohol dehydrogenase b. oxidoreductase
c. DNA (Topo)isomerase c. Isomerase
d. Pepsin d. hydrolase
e. Ligase
e. Tyrosine-tRNA synthetase f. Transferase
f. Pyruvate kinase g. Hydrolase
g. Acetylcholinesterase h. Transferase

h. Aspartate amino transferase

2. Lipases are enzymes that are (more or less) specific than ACE
3. Of the two main models used to explain enzymatic action, the ____________ model is
regarded as more flexible than the ____________ model.
4. A number of enzymes require a nonprotein component called a ____________ or
____________ to exhibit enzymatic activity.
5. Trypsinogen is an example of a ____________ that can only be a ____________ by
removal of a portion of the protein.
6. If the enzyme concentration is tripled, the reaction rate will ____________
7. Enzymes change the ____________ of the reaction, but do not change the
____________ concentrations in the reaction.
23.1 What Are Enzymes?
a. All enzymes are globular proteins.
b. Some enzymes are made out of DNA.
c. Enzymes are biological catalysts.
d. Enzymes exhibit substrate specificity.
e. Trypsin is an enzyme that catalyzes the cleavage of peptide bonds.
f. Trypsin makes the free energy of activation of the reaction more favorable
g. Lipases catalyzes the cleavage of fatty acids off of triacylglycerols.

23.2 How are Enzymes Named and Classified?

a. Non-protein parts of enzymes are called cofactors
b. The polypeptide portion of an enzyme is called an apoenzyme.
c. Heavy metal cofactors are called coenzymes.
d. The molecules that the enzyme binds to and converts to products are called
substrates.
e. When an inhibitor binds to the active site, it is called a non-competitive inhibitor
f. In a reaction with only one substrate, a competitive inhibitor and the substrate
cannot bind at the same time.

23.4 What Factors Affect Enzyme Activity?

a. If you double the amount of enzyme, the rate of the enzyme-catalyzed reaction
doubles.
b. If you double the amount of substrate, the rate of the enzyme-catalyzed reaction
doubles.
c. If you double the temperature of an enzyme catalyzed reaction, the reaction rate
will double.
d. An enzyme has a characteristic profile of rate versus pH.

23.6 How Are Enzymes Regulated?

a. Feedback control means that the product of a reaction inhibits the enzyme that
catalyzed its production
b. An enzyme that is produced initially in an inactive form is called a zymogen.
c. The zymogen form of an enzyme and the active form are easily interconverted
d. Allosteric enzymes often have multiple subunits.
e. A substance that binds to an allosteric enzyme at a location other than the active
site is called a regulator
f. Glycogen phosphorylase is an allosteric enzyme
g. Glycogen phosphorylase is regulated by phosphorylation.
h. Kinases and phosphatases are often used to modify enzymes.
i. Enzymes that have multiple forms in different tissues are called isozymes.
j. In a given organism, there are 8 isozymes of lactate dehydrogenase.
k. Isozymes of lactate dehydrogenase differ in their electrophoretic mobility.