Biochem - Biochem - Enzyme and Kinetics [2] Flashcards
1
Q
- 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
2
Q
- 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
- (ν0−νi)/ν0(ν0−νi)/ν0
3
Q
- The rate equation in competitive inhibition based on Michaelis Menten equation is given by
A
- rmaxS/(Kmt(1+I/Ki)+S))rmaxS/(Kmt(1+I/Ki)+S))
4
Q
- Classical noncompetitive inhibition is obtained only under
A
- Rapid equilibrium conditions
5
Q
- 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
6
Q
- For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vmax) observed at [S] = 2 KM will be
A
- 0.66
7
Q
- Predominantly uncompetitive inhibition may be called when
A
- Competitive inhibition is smaller than uncompetitive inhibition
8
Q
- 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
- 13.54μ moles liter-1min-1
9
Q
- The rate equation in non-competitive inhibition based on Michaelis Menten equation is given by
A
- rmaxS/(Km+S)(1+I/Ki)rmaxS/(Km+S)(1+I/Ki)
10
Q
- Which of the following statement(s) regarding enzymes, is/are false?
A
- Enzymes provide activation energy for reactions
11
Q
- The slope of Lineweaver Burk plot for Michaelis Menten equation is
A
- KmVmaxVmaxKm
12
Q
- The initial velocity, V0, of an enzyme catalyzed reaction reaches Vmax as
A
- [S]=10∗KM[S]=10∗KM
13
Q
- The usual method(s) to solve rate equation of simple enzyme kinetics is/are
A
- All of these
14
Q
- Michaelis Menten equation can also be written as
A
- (-Cs)/r = (Cs/rmax)+(Km/rmax)
15
Q
- Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?
A
- The product releasing step
16
Q
- When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about
A
- 0.5 * Vmax
17
Q
- A classical noncompetitive inhibitor has
A
- No effect on substrate binding
18
Q
- The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site
A
- Catalyzes a chemical reaction
19
Q
- Enzymes are basically
A
- Proteins
20
Q
- Which of the following refers to pseudo steady state?
A
- d(CES)/dt = 0
21
Q
- Most enzymes work by
A
- Decreasing energy of activation
22
Q
- Which category of enzymes belongs to class 5 in the international classification?
A
- Isomerases
23
Q
- Lock and key theory is based on the compatibility of
A
- Enzyme and substrate
24
Q
- When an enzyme is functioning at Vmax, the rate of the reaction is limited by
A
- The rate at which the enzyme can convert substrate to product
25
Q
- The equation for the rate of product formation for simple enzyme reaction is given by
A
- rp=rmax Cv/(Km+Cs)rp=rmaxCv/(Km+Cs)
26
Q
- When [S] = 0.1 * KM, the velocity of an enzyme catalyzed reaction is about
A
- 0.1 * Vmax