moo Flashcards
(509 cards)
A competitive inhibitor of an enzyme is usually
a. a highly reactive compound
b. a metal ion such as Hg2+ or Pb2+
c. structurally similar to the substrate.
d. water insoluble
structurally similar to the substrate.
Linear inhibition is sometimes called as
a. complete inhibition
b. incomplete inhibition
c. partial inhibition
d. mixed inhibition
complete
The types of inhibition pattern based on
Michaelis Menten equation are
a. competitive
b. non-competitive
c. uncompetitive
d. all of the above
all of the above
The effect of non-competitive inhibition on a
Lineweaver-Burk Plot is that
a. it can move the entire curve to the right
b. it can change the y-intercept
c. it can change the x-intercept
d. all of thes
can change the y-intercept
The rate-determining step of Michaelis Menten
kinetics is
a. the complex formation step
b. the complex dissociation step to produce
product
c. the product formation step
d. Both (a)and(c)
the complex dissociation step to produce
product
In competitive inhibition a factor is obtained
from the measurement of
a. Vmax
b. KM
c. Y-intercept in Lineweaver-Burk Plot
d. None of these
Km
Which of these proteases is not a cysteine active
site protease?
a. Calpain
b. Cathepsin D
c. Papain
d. None of the above
cathepsin D
Given an enzyme with a Km = 10m M and Vmax
= 100 m mol/min. If [S] = 100 m M, which of
the following will be true?
a. A 10-fold increase in Vmax would increase
velocity 10-fold y
b. A 10-fold decrease in Km would increase
velocity
c. Both (a) and (b)
d. A 10-fold increase in Vmax would decrease
velocity 20-fold
A 10-fold increase in Vmax would increase
velocity 10-fold y
The conformational change in an enzyme after
the substrate is bound that allows the chemical
reaction to proceed, can be explained by
a. induced fit
b. transition
c. fit and fine
d. Pasteur
INDUCED FIT
. The active site of an enzyme remains
a. at the center of globular proteins
b. rigid and does not change shape
c. complementary to the rest of the molecule
d. none of the above
none of the above
Which category of enzymes belongs to class
two in the international classification?
a. Hydrolases
b. Ligases
c. Transferases
d. Isomerase
transferases
The Woolf-Augusteinsson-Hofstee plot of ν
versus ν/[S] and the Eadie-Scatchard plot of
ν/[S] versus ν do not involve reciprocals of ν
therefore are considered to be more reliable
when the error in v is
a. non-significant
b. significant
c. nothing to do with the reliability
d. non-significant in selected cases
significant
The relationship between Keq, Km and Vmax is
known as
a. Haldane equation
b. Michaelis Menten equation
c. Numerical solution approach
Haldane
. The reciprocal equation for non-competitive
inhibition can be arranged to the equation for
the
a. Dixon plot
b. Woolf-Augusteinsson-Hofstee plot
c. Eadie-Scatchard plot
d. Hanes-Woolf plot
Dixon plot
Which of the following statements is true for
enzymatically catalyzed reaction?
a. The activation energy of the reaction is
lowered so that a larger proportion of the
substrate qualifies to overcome it
b. Additional substrate molecules are
energized to overcome the activation
energy of the reaction
c. The activation energy of the reaction is
increased, thus decreasing the likelihood
that any substrate molecules will overcome
it
d. The activation energy of the reaction is
lowered so that fewer substrate molecules
can overcome it
The activation energy of the reaction is
lowered so that a larger proportion of the
substrate qualifies to overcome it
Which of the following common drugs is not a
specific enzyme inhibitor?
a. Iodine
b. Methotrexate
c. Sulfanilamide
d. Penicillin
Iodine
In a Lineweaver-Burk Plot, competitive
inhibitor shows which of the following effect?
a. It moves the entire curve to right
b. It moves the entire curve to left
c. It changes the x-intercept
d. It has no effect on the slope
changes the x-intercept
Which of the following statements is not true?
a. Enzymes are proteins that bind to specific
substrates and increase the velocity of
reactions involving those substrates
b. Enzymes function by overcoming the
activation energy barrier of a reaction
c. Enzymes make thermodynamically
favorable reactions to proceed; they cannot
make unfavorable reactions to occur
d. Enzymes only function when they are in
intact cells
Enzymes only function when they are in
intact cells
Non-competitive inhibitor of an enzyme
catalyzed reaction
a. decreases Vmax
b. binds to Michaelis complex (ES)
c. both (a) and (b)
both
An enzyme and a reactant molecule maintain
relationship as
a. a temporary association
b. an association stabilized by a covalent bond
c. one in which the enzyme is changed
permanently
d. non complementary binding
temporary association
An enzyme is assayed at an initial substrate
concentration of 2 x 10-5M. In 6-minute, half
of the substrate is used. The Km for the
substrate is 2 x 10-3M. The value of k in minute
is
a. 0.115
b. 0.42
c. 0.093
d. 6.693
0.115
The plot commonly used for determining the
value of Vmax is
a. Lineweaver Burk plot
b. Langmuir plot
c. Eadie Hofstee plot
d. all of these
all of these
Quasi steady state is also known as
a. Michaelis Menten approach
b. Briggs-Haldane approach
c. Pseudo steady state
d. all of the abov
Pseudo steady state
Which of these enzymes contains a Zinc (Zn)
ion?
a. Carboxypeptidase A
b. Phosphorylase B kinase
c. Tyrosine hydroxylase
d. Phosphodiesterase
Carboxypeptidase A