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Chemical Kinetics
Assignment-8
1. The expression for the equilibrium constant (Keq) for the
enzyme catalyzed reaction given below, is
ky
E+ § —— Es = Pte
“he
kyuks kaks 0 fake
“A kok, ®) kesky mM A
2. Inan enzyme-catalysed reaction gf)
0? mol dm®, the magnitude of
over number using Michaelis-Menten
1, 3.42x10* st
iol dnv3 s!; 3.42104 st
(C) 3.42x10* mol dm? s*; 3.42x10° s!
(D) 3.42x104 mol dm s"!; 3.4210? st
3. The slope and intercept obtained from (1/Rate) against
(1/substrate concentration) of an enzyme catalyzed reaction are
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300 and 2 x 10°, respectively. The Michaelis-Menten constants of
the enzyme in this reaction is
(a) S x 10°M (b) 5x 10°M
(c) 1.5 x 103M (d) 1.5x 103M
4. For an enzyme-substrate reaction,
ky ky
ES ES ———>
E+s
ka
The slope and the intercept of the plot and 1/[S] are
M and k.j/k2 =
‘its of M’! s") [r is the
centration of the enzyme]
(c) 1 x 108 (d) 1 x 108
er-Burk plot of (initial rate)! vs ( initial substrate
for an enzyme catalyzed reaction following
Michaelis-Menten mechanism, the y-intercept is 5000 M''s. If the
initial enzyme concentration is 1 x 10° M, the turnover number is
(a) 25x10; (10x10. (c)25x10. (20x10:
6. For an enzyme catalyzed reaction, a Lineweaver-Burk plot gave
the following data:
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Slope = 40s, intercept = 4 (mmol dm? s"'y!
If the initial concentration of enzyme is 2.5 x 10° mol dm, what
is the catalytic efficiency (dm* mols") of the reaction?
(a) 10° (b) 10° (c) 107 (d) 104
7. For an enzyme-substrate reaction the Michaeli 0.042
mol dm. The rate of this reaction is Pa 3st
when the substrate concentration is 0.89 mol jaximum
velocity(mol dm® s"') of this enzymolysit
(a) 2.52.x 103 (b) 2.45 x 105 f (d) 1.31 x 10%
9. For an enzyme substrate reaction, a plot between I/v and 1/[S]
yields a slope of 40s. If the enzyme concentration is 2.5 uM, then
the catalytic efficiency (Lmol"'s") of the enzyme is
(a) 40 (b) 104 (c) 107 (d) 108
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