Study Questions

ENZYMES
Answer True(T) or False (F)
Which of the following statements is NOT characteristic of allosteric
enzymes?
a. They are often composed of subunits.(T)
b. Allosteric enzymes are regulated by molecules called effectors(T)
c. The binding of a positive allosteric effector results in an increase in
enzymic activity(T)
d. They frequently catalyze the slowest step in metabolic pathway.(T)
e. They follow Michaelis-Menten kinetics.(F)
The rate of an enzyme-catalyzed reaction can best be described as
a. Proportional to the substrate concentration.(T)
b. Reaction velocity is proportional to enzyme concentration at all
concentrations of substrate.(T)
c. independent of enzyme concentration(F)
d. Zero order with respect to substrate (F)
e. Increased in the presence of a noncompetitive inhibitor(F)
Which statement is CORRECT?
a. Enzymes are small molecules that are heat stable(F).
b. Enzymes affect rates of reactions in the forward and reverse
direction.(T)
c. Enzymes will determine whether a reaction will take place.(F)
d. Enzymes are permanently altered following the conversion of
substrate to product.(F)
e. Enzymes are used as therapeutic agents.(T )
Competitive inhibitors are commonly used in chemotherapy because:
a. The inhibitors decrease the total amount of substrate.(F)
b. The inhibitors alter the enzymes when they bind and decrease
the maximal velocity (Vm) of the reaction.(F)
c. The inhibitors resemble the structure of the product and inhibit
the reaction by negative feedback.(F)
d. The inhibitors do not bind the active site of the enzyme.(F)
e. The inhibitor binds only to the active site and increases the
Michaelis constant (Km).(T)
Malonate inhibits succinic dehydrogenase because it
a. Binds irreversibly to the active site.(F)
b. Covalently modifies the enzyme.(F)

c. Chelates a metal ion required by the enzyme.(F)

d. Displaces the FAD coenzyme(F)
e. Resembles succinate but can not react.(T)

A drug which acts as a noncompetitive inhibitor

a. increases the steady-state concentration of the ES complex.(F)
b. has a structure similar to a substrate(F)
c. acts by removing active enzyme from the substrate pool.(T)
d. is usually irreversible.(F)
e. combines with allosteric sites on the enzyme.(T)
Which of the following is true for enzymes?
a. Lactate dehydrogenase catalyze oxidation and reduction processes.
(T)
b. Transaminases catalyze the transfer of amino group from an amino
acid to alpha ketoglutaric acid.(T)
c. Carbamoyl phosphate synthetase, an enzyme catalyzes biosynthetic
reaction providing carbamoyl phosphate by cleavage of two
molecules of ATP.(T)
d. Triose isomerase catalyzes conversion of dihydroacetone
phosphate to D-glyceraldehyde-3-phosphate.(T)
e. Aldolase catalyzes the cleavage of glyceraldehydes-3-phosphate to
fructose 1, 6-phosphate(F)
Notes
*Zero order means that the reaction velocity is independent of substrate
concentration. This is observed only when the substrate concentration is
much greater than Km.
Km(Michalies constant): is a constant, characteristic of an enzyme
and a particular substance, and reflects the affinity of the enzyme
for that substrate.
Slowest step: an early committed step in that pathway.
Allosteric binding sites: Enzymes are regulated by molecules
called" effectors" also called modifiers or modulators that
noncovalently bind at site other than active site.
Effectors that inhibit enzyme activity are termed "negative
effectors"
Effectors that increased enzyme activity are called" positive
effectors"