BCE Flashcards
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
C
Linear inhibition is sometimes called as
A. complete inhibition
B. incomplete inhibition
C. partial inhibition
D. mixed inhibition
A
The types of inhibition pattern based on Michaelis Menten
equation are
A. competitive
B. non-competitive
C. uncompetitive
D. all of the above
D
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 these
B
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)
B
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
B
Which of these proteases is not a cysteine active site protease?
A. Calpain
B. Cathepsin D
C. Papain
D. None of the above
B
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
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
A
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
D
Non-competitive inhibitor of an enzyme catalyzed reaction
A. decreases Vmax
B. binds to Michaelis complex (ES)
C. both (a) and (b)
D. can actually increase reaction velocity in rare cases
C
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
A
Which category of enzymes belongs to class two in the
international classification?
A. Hydrolases
B. Ligases
C. Transferases
D. Isomerase
C
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
B
The relationship between Keq, Km and Vmax is known as
A. Haldane equation
B. Michaelis Menten equation
C. Numerical solution approach
D. Gibbs-Helmholtz equation
A
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
A
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
a fewer substrate molecules can overcome it
A
Which of the following common drugs is not a specific enzyme
inhibitor?
A. Iodine
B. Methotrexate
C. Sulfbnilamide
D. Penicillin
A
The enzyme inhibition can occur by
A. reversible inhibitors
B. irreversible inhibitors
C. Both (a) and (b)
D. None of these
C
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
C
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
D
An enzyme is assayed at an initial substrate concentration of 2 x
10-5M. In 6 minutes, 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
A
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
D
Quasi steady state is also known as
A. Michaelis Menten approach
B. Briggs-Haldane approach
C. Pseudo steady state
D. all of the above
C
Which of these enzymes contains a Zinc (Zn) ion?
A. Carboxypeptidase A
B. Phosphorylase B kinase
C. Tyrosine hydroxylase
D. Phosphodiesterase
A
A noncompetitive inhibitor of an enzyme-catalyzed reaction
A. increases KM and increases Vmax
B. increases KM and reduces Vmax
C. reduces KM and increases Vmax
D. reduces KM and reduces Vmax
B
An allosteric inhibitor of an enzyme usually
A. participates in feedback regulation
B. denatures the enzyme
C. is a hydrophobic compound
D. causes the enzyme to work faster
A
Which of the following activity is possible by transferases?
A. Transfer of methyl groups
B. Transfer of glycosyl group
C. Both (a) and (b)
D. None of these
C
A classical uncompetitive inhibitor is a compound that binds
A. reversibly to the enzyme substrate complex yielding an
inactive ESI complex
B. irreversibly to the enzyme substrate complex yielding
an inactive ESI complex
C. reversibly to the enzyme substrate complex yielding an
active ESI complex
D. irreversibly to the enzyme substrate complex yielding
an active ESI complex
A
Which graphical method is used to determine an enzyme
degree of cooperativity?
A. Hill plot
B. Koshland curve
C. Michaelis-Menten hyperbola
D. Can not be determined
A
The ratio of the amount of a protein present in a sample, which
is used as a measure of purification, is known as
A. specific activity
B. relative activity
C. purity ratio
D. all of these
A
If a reaction occurs in the absence of inhibitor with rate ν0 and in
the presence of inhibitor with rate νi, the degree of inhibition is
defined as
A. (ν0 - νi)/ν0
B. (ν0 + νi)/ν0
C. (ν0νi)/ν0
D. (ν0-νi)/νi
A
The rate equation in competitive inhibition based on Michaelis
Menten equation is given by
A. rmaxS/(Km (1+I/Ki)+S))
B. rmaxE/(Km (1+I/Ki)+S))
C. rmaxI/(Km (1+I/Ki)+S))
D. rmaxS/(Km (1+I/Ki))
A
Classical noncompetitive inhibition is obtained only under
A. slow equilibrium conditions
B. moderate equilibrium conditions
C. rapid equilibrium conditions
D. non-equilibrium conditions
C
In the steady state the material balance equation for any
component of a system is
A. rate of addition + rate of removal - rate of formation = 0
B. rate of addition - rate of removal + rate of formation = 0
C. rate of addition + rate of removal + rate of formation =
0
D. none of the above
B
For an enzyme that displays Michaelis-Menten kinetics, the
reaction velocity (as a fraction of Vmax) observed at [S] = 2
KM will be
A. 0.09
B. 0.33
C. 0.66
D. 0.91
C
Predominantly uncompetitive inhibition may be called when
A. competitive inhibition is greater than uncompetitive
inhibition
B. competitive inhibition is smaller than uncompetitive
inhibition
C. competitive inhibition is equal to uncompetitive
inhibition
D. none of the above
A
The rate equation in non-competitive inhibition based on
Michaelis Menten equation is given by
A. rmaxS/(Km + S)(1+I/Ki)
B. rmaxE/(Km (1+I/Ki)+S))
C. VmaxS/(Km + S)(1+I/Ki)
D. rmaxS/Km
A
Which of the following statement(s) regarding enzymes, is/are
false?
A. Enzymes are always proteins that function as catalysts
B. Enzymes provide activation energy for reactions
C. Enzyme activity can be regulated
D. Enzymes may be used many times for a specific
reaction
B
The slope of Lineweaver Burk plot for Michaelis Menten
equation is
A. Vmax/Km
B. Km/Vmax
C. 1/Km
D. Km.Vmax
B
The initial velocity, V0, of an enzyme catalyzed reaction reaches
Vmax as
A. [S] = KM
B. [S] = 10 * KM
C. 1/[S] = 1/KM
D. 1/[S] → 0
D
The usual method(s) to solve rate equation of simple enzyme
kinetics is/are
A. Michaelis Menten approach
B. Briggs-Haldane approach
C. Numerical solution approach
D. all of these
D
Michaelis Menten equation can also be written as
A. (-Cs)/r = (Cs/rmax)+(Km/rmax)
B. 1/r = (1/rmax)+(Km/(rmax.Cs))
C. r = rmax-(Km.r/Cs)
D. All of these
D
Which of the following step is assumed to be the slowest step in
the Michaelis Menten equation?
A. The substrate consuming step
B. The product releasing step
C. Formation of enzyme substrate complex
D. None of these
B
When substrate [S] = KM (Michaelis-Menten constant), the
velocity of an enzyme catalyzed reaction is about
A. 0.1 * Vmax
B. 0.2 * Vmax
C. 0.5 * Vmax
D. 0.9 * Vmax
C