Biochemical Engineering Flashcards
(505 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
c. structurally similar to the substrate.
Linear inhibition is sometimes called as
a. complete inhibition
b. incomplete inhibition
c. partial inhibition
d. mixed inhibition
a. complete inhibition
The types of inhibition pattern based on Michaelis Menten equation are
a. competitive
b. non-competitive
c. uncompetitive
d. all of the above
d. 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 these
b. it 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)
b. 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
b. KM
Which of these proteases is not a cysteine active site protease?
a. Calpain
b. Cathepsin D
c. Papain
d. None of the above
b. 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. 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
a. 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
d. none of the above
Which category of enzymes belongs to class two in the international classification?
a. Hydrolases
b. Ligases
c. Transferases
d. Isomerase
c. 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
b. significant
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. Haldane equation
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. 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
a. 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
a. Iodine
The enzyme inhibition can occur by
a. reversible inhibitors
b. irreversible inhibitors
c. Both (a) and (b)
d. None of these
c. Both (a) and (b)
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. It 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
d. 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)
d. can actually increase reaction velocity in rare cases
c. both (a) and (b)
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. a 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
a. 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
d. 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 above
c. Pseudo steady state