Biochem - Biochem - Enzyme and Kinetics [2] Flashcards

1
Q
  1. The ratio of the amount of a protein present in a sample, which is used as a measure of purification, is known as
A
  1. Specific activity
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2
Q
  1. If a reaction occurs in the absence of inhibitor with rate v0 and in the presence of inhibitor with rate vi, the degree of inhibition is defined as
A
  1. (ν0−νi)/ν0(ν0​−νi​)/ν0​
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3
Q
  1. The rate equation in competitive inhibition based on Michaelis Menten equation is given by
A
  1. rmax⁡S/(Kmt(1+I/Ki)+S))rmax​S/(Kmt​(1+I/Ki​)+S))
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4
Q
  1. Classical noncompetitive inhibition is obtained only under
A
  1. Rapid equilibrium conditions
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5
Q
  1. In the steady state the material balance equation for any component of a system is
A
  1. Rate of addition + rate of removal - rate of formation = 0
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6
Q
  1. For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vmax) observed at [S] = 2 KM will be
A
  1. 0.66
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7
Q
  1. Predominantly uncompetitive inhibition may be called when
A
  1. Competitive inhibition is smaller than uncompetitive inhibition
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8
Q
  1. An enzyme has a Km of 4.7 x 10-5M. If the Vmax of the preparation is 22m moles liter-1 min-1, what velocity would be observed in the presence of 2.0 x 10-4M substrate and 5.0 x 10-5M of a competitive inhibitor?
A
  1. 13.54μ moles liter-1min-1
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9
Q
  1. The rate equation in non-competitive inhibition based on Michaelis Menten equation is given by
A
  1. rmax⁡S/(Km+S)(1+I/Ki)rmax​S/(Km​+S)(1+I/Ki​)
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10
Q
  1. Which of the following statement(s) regarding enzymes, is/are false?
A
  1. Enzymes provide activation energy for reactions
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11
Q
  1. The slope of Lineweaver Burk plot for Michaelis Menten equation is
A
  1. KmVmax⁡Vmax​Km​​
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12
Q
  1. The initial velocity, V0, of an enzyme catalyzed reaction reaches Vmax as
A
  1. [S]=10∗KM[S]=10∗KM​
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13
Q
  1. The usual method(s) to solve rate equation of simple enzyme kinetics is/are
A
  1. All of these
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14
Q
  1. Michaelis Menten equation can also be written as
A
  1. (-Cs)/r = (Cs/rmax)+(Km/rmax)
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15
Q
  1. Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?
A
  1. The product releasing step
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16
Q
  1. When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about
A
  1. 0.5 * Vmax
17
Q
  1. A classical noncompetitive inhibitor has
A
  1. No effect on substrate binding
18
Q
  1. The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site
A
  1. Catalyzes a chemical reaction
19
Q
  1. Enzymes are basically
20
Q
  1. Which of the following refers to pseudo steady state?
A
  1. d(CES)/dt = 0
21
Q
  1. Most enzymes work by
A
  1. Decreasing energy of activation
22
Q
  1. Which category of enzymes belongs to class 5 in the international classification?
A
  1. Isomerases
23
Q
  1. Lock and key theory is based on the compatibility of
A
  1. Enzyme and substrate
24
Q
  1. When an enzyme is functioning at Vmax, the rate of the reaction is limited by
A
  1. The rate at which the enzyme can convert substrate to product
25
Q
  1. The equation for the rate of product formation for simple enzyme reaction is given by
A
  1. rp=rmax Cv/(Km+Cs)rp​=rmax​Cv​/(Km​+Cs​)
26
Q
  1. When [S] = 0.1 * KM, the velocity of an enzyme catalyzed reaction is about
A
  1. 0.1 * Vmax