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- Henzyme Kinetics I
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Problem 1

Determine the initial rate of product (P) formation from enzyme X and

substrate Y that form the complex XY. The reaction kinetics is given by

Solution:

Michaelis-Menten approach : The rate of reaction is given by

rp = k f2 C XY k b2 C P C X (1.1)

C X0 = C X + C XY

Si

Since enzyme is

i preserved

d

(1.2)

S b tit ti equation

Substituting ti (1.2)

(1 2) in

i (1.1)

(1 1) we gett

rp = (k f2 + k b2 C P )C XY k b2 C P C X0 (1.3)

kf1

C XY = CXCY (1.4)

k b1

Substituting equation (5) in equation (3) for CX and rearranging for CXY yields

CX0 CS (1.5)

CXY =

k b1

CS

k f1

Substituting equation (6) into equation (2) gives

k b2 k b1 (1.6)

k f2 C X0 C Y C P

k f2 k f1

rp =

k b1

+ CS

k f1

Equation (7) is in Michaelis-Menten form of equation, where

rMax = k f2 C XO

and

k b1

KM =

k f1

Problem 2

Determine

D t i the

th initial

i iti l rate

t off product

d t (P) formation

f ti from

f enzyme X andd

substrate Y that form the complex XY. The reaction kinetics is given by

Solution : We can write the mass balance for the intermediates and product as:

d[(XY )1 ] (2.1)

= k b1 [X ][Y ] (k f1 + k 2 )[(XY )1 ]

dt

d[(XY )2 ]

= k 2 [(XY )1 ] (k f3 )[(XY )2 ] (2.2)

dt

d[P ]

= (k f3 )[(XY )2 ] (2.3)

dt

k f2

where k2 =

k b2

Assuming [(XY)1] and [(XY)2] are in steady state, we can eliminate

[(XY)2] from equation (2.4)

k f1 [X ][Y ]

[(XY )1 ] = (2.4)

k b1 + k 2

[(XY )2 ] = k2

[(XY )1 ] = k 2 k 1 [X][Y] ( )

(2.5)

k f3 k f3 k b1 + k 2

d[P] k 2 k f1 [X ][Y ]

rp = = k f3 (2 6)

(2.6)

dt k f3 k b1 + k 2

Since the enzyme is preserved

[X 0 ] = [X] + [(XY )1 ] + [(XY )2 ] (2.7)

Substituting for [X] in terms of [X0] in equation (2.8) we get

k 2 k f3

[X][Y]

(k 2 + k f3 )

rp = (2.8)

k f3 k b1 + k 2

+ [Y ]

k 2 + k f3f k f1f

Hence the KM and Vmax values are reduced by the ratio kf3/(k2+ kf3),

resulting from the presence of the second intermediate [(XY)2].

]

Problem3

The loading of O2 to Hb (hemoglobin) follows a cooperative binding

and is given by

from measurements of Hb (O2)n

Solution:

Total hemoglobin concentration is given by

[Hb]T = [Hb] + [Hb(O 2 )n ] = Constant

[Hb(O 2 )n ] = [Hb(O 2 )n ]

[Hb]T [Hb] + [Hb(O 2 )n ]

(3.1)

Given reaction is

Hb + nO 2 Hb(O 2 )n

Assuming steady state, therefore

K 1 [Hb][O 2 ] = K 2 [Hb(O 2 )n ] (3.2)

n

K1

[Hb][O 2 ]n

[Hb(O 2 )n ] = K 2 (3.3)

[Hb]T [Hb] + K 1 [Hb][O 2 ]n

K2

As concentration is directlyy proportional

p p to ppressure,, we can write equation

q

(3.3) as

K1 n n

PO 2

[Hb(O 2 )n ] = K 2 (3.4)

[Hb]T K

1 + 1 n POn 2

K2

After the algebraic manipulations

[Hb]T K1

+ P n

O

K 2 n 2

oxygen is given by Hill Equation.

Hill Equation:

POn2

SO2 = (3.6)

P +Pn

50

n

O2

Therefore

SO2 =

[Hb(O 2 )n ]

(3 7)

(3.7)

[Hb]T

From equation (3.6) and equation (3.7)

POn 2

SO 2 = (3.8)

K1

+ P n

O2

K 2 n

Rearranging we get

S O 2 (3 9)

(3.9)

K1

=

n

PO2

1 S O 2

n

K 2

Taking log on both side, we get

S O 2 K1

ln = ln

K n + n ln PO 2

1 S O 2 2 (3 10)

(3.10)

S O 2

Thus a logarithmic plot of versus PO2 will give a straight line of

slope n 1 S O 2

Problem 4

An inhibitor Y is added to the enzymatic reaction at a level of 1.2 gm/L. Their data

were obtained for KM=10 gm/L.

Rate Substrate

1.8 20

1.3 9.8

0.98 6.7

0.8 5.1

0.67 4.2

0.6 3.2

0.45 2.6

a. Identify

Id tif ththe ttype off iinhibition

hibiti (i(i.e. C

Competitive,

titi N Non-competitive

titi or

Uncompetitive)

b.

Solution: Lets us assume that the given enzymatic reaction is

inhibited by competitive inhibition.

inhibition For an instance of competitive

inhibition the Lineweaver-Burke equation is

1 K M 1 [I] 1

= 1 + + (4 1)

(4.1)

V VMax [S] K i VMax

1 1

So we pplot versus to gget the values of VMax and Ki

V S

From fig.4.1 we get Vmax=1.8181. Slope = 2.33826, therefore

1 [I]

1 + = 2.3383

VMax Ki

Hence inhibitor constant Ki = -2.087

enzyme inhibitor complex. A lower value of Ki denotes a stronger

inhibition. So as the value of Ki (-2.087) is negative our assumption

was correct and it is a competitive inhibition.

adding additional substrate.

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