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2.3 In some enzyme- catalyzed reaction, multiple complexes are involved as follows:

S + E ↔ ( ES )1

( ES )1 ↔ ( ES )2

( E )2 → P + E

REQUIRED: Develop a rate expression using

a. Michaelis Menten approach

b. The Briggs Haldane approach

SOLUTION :

−dcs dcp

rp = = = ksCes − k4CpCe

dt dt

Ceo = Ce = Ces ; Ce = Ceo – Ces

rp = k3Ces – k4CpCeo + k4CpCes

rp = ( k3 + k4 ) Ces – k4CpCeo

k1 CsCe = k2Ces

k1(Cs)(Ceo-Ces) = k2Ces

k1CsCeo-k1CsCes=k2Ces

k2Ces + k1CsCes = k1CsCeo

k1 CsCeo

Ces =

k2 + k1Cs

CeoCs

Ces =

k2

+ Cs

k1

CeoCs

rp = ( k3 + k4Cp) k2 - k4Ceo

+Cs

k1

k2

(ks+k4Cp)(CeoCs)− ( Cs ) ( k4CpCeo )

k1

rp = k2

+Cs

k1

k2k4CpCeo

k3CeoCs + k4CeoCpCs − − k4CpCesCs

rp = k1

k2

+ Cs

k1

k2k4CpCeo

k3CeoCs −

rp = k1

k2

+ Cs

k1

k2k4

Ceo (k3cs − Cp)

rp = k1

k2

+ Cs

k1

Ce=Ceo=Ces

k1CsCeo

k2

+ Cs

k1

CsCeo

k2

+ Cs

k1

ANSWER

k3CeoCs rmaxCx

=

k2

+ Cs Km + Cs

k1

The Briggs Haldane

−dcs dcp

= = k3Ces

dt dt

−dcs

= k1CsCe − k2Ces − k3Ces = 0

dt

Ceo = Ce + Ces

K1Cs ( Ceo-Ces )=k2Ces-k3Ces

K1CsCeo-k1CsCes-k3 ; Ces=0

K1CsCes+k2Ces+k3Ces = k1CsCeo

k1CsCeo

Ces =

k1Cs + k2 + k3

CsCeo

Ces =

k3 + k2

+ Cs

k1

= =

dt dt k3 + k2

+ Cs

k1

rmaxCs

rp= KmCs

CHAPTER 2: ENZYME KINETICS

2.4 Eadie (1942) measured the initial reaction rate of hydrolysis of acetylcholine (substrate) by

dog serum (source of enzyme) and obtained the following data:

mol/L mol/L·min

0.0032 0.111

0.0049 0.148

0.0062 0.143

0.0080 0.166

0.0095 0.200

Evaluate the Michaelis-Menten kinetic parameters by employing (a) the Langmuir plot, (b) the

Lineweaver-Burk plot, and (c) the Eadie-Hofstee plot.

Required: Michaelis-Menten kinetic parameters

Solution:

a. Langmuir

CS KM 1

= + CS

r rmax rmax

x, CS y, CS/r

0.0032 0.0032/0.111

0.0049 0.0049/0.148

0.0062 0.0062/0.143

0.0080 0.0080/0.166 rmax = 0.3018 mol/L·min

0.0095 0.0095/0.200 KM = 5.7721 x 10-3 mol/L

b. Lineweaver-Burk

1 1 KM 1

= +

r rmax rmax CS

x, 1/CS y, 1/r

1/0.0032 1/0.111

1/0.0049 1/0.148

1/0.0062 1/0.143

1/0.0080 1/0.166 rmax = 0.2752 mol/L·min

1/0.0095 1/0.200 KM = 4.7303 x 10-3 mol/L

c. Eadie-Hofstee

r

r = rmax - KM

CS

x, r/CS y, r

0.111/0.0032 0.111

0.148/0.0049 0.148

0.143/0.0062 0.143

0.166/0.0080 0.166 rmax = 0.2645 mol/L·min

0.200/0.0095 0.200 KM = 4.2731 x 10-3 mol/L

CHAPTER 2: ENZYME KINETICS

2.7 The KM value of an enzyme is known to be 0.01 mol/L. To measure the maximum reaction rate

catalyzed by the enzyme, you measured the initial rate of the reaction and found that 10 percent of

the initial substrate was consumed in 5 minutes. The initial substrate concentration is 3.4x10 -4

mol/L. Assume that the reaction can be expressed by the Michaelis-Menten kinetics.

Given:

KM = 0.01 mol/L @t=5 minutes

Cso= 3.4x10-4 mol/L 10 percent was consumed

b.) Cs @t=15 minutes

Solution:

K M ln 𝐶𝑠𝑜

𝐶𝑠

+ (𝐶𝑠𝑜−𝐶𝑠) = 𝑟𝑚𝑎𝑥 𝑡

mol

0.01 1

ln 0.9 + (1−0.9)(3.4x10−4)

𝑚𝑜𝑙

𝐿

= 𝑟𝑚𝑎𝑥 (5𝑥60)𝑠

L

@t= 15 minutes

K M ln 𝐶𝑠𝑜

𝐶𝑠

+ (𝐶𝑠𝑜−𝐶𝑠) = 𝑟𝑚𝑎𝑥 𝑡

mol kmol

0.01 ln 3.4𝑥10−4

𝐶𝑠

+ (3.4𝑥10−4−𝐶𝑠)

𝑚𝑜𝑙

𝐿

= (3.6254x10 − 6 m3 s ) (15𝑥60)𝑠

L

CHAPTER 2: ENZYME KINETICS

2.8 A substrate is converted to a product by the catalytic action of an enzyme. Assume that the

Michaelis-Menten kinetic parameters for enzyme reaction are:

KM = 0.03 mol/L

rmax= 13 mol/ L min

a. What should be the size of a steady-state CSTR to convert 95 percent of incoming

substrate (Cso= 10 mol/L) with a flow rate of 10 L/h?

b. What should be the size of the reactor if you employ a plug-flow reactor instead of the

CSTR in part (a)?

Given: Req'd:

KM = 0.03 mol/L a)VCSTR

rmax= 13 mol/ L min b) VPFR

Cso= 10 mol/L

F= 10 L/h

Sol'n:

a)

𝐹 1 𝑟𝑚𝑎𝑥 𝐶𝑠

= =

𝑉 𝜏 (𝐶𝑠𝑜 − 𝐶𝑠)(𝐾𝑚 + 𝐶𝑠)

𝐹

𝑉=

𝑟𝑚𝑎𝑥 𝐶𝑠

(𝐶𝑠𝑜 − 𝐶𝑠)(𝐾𝑚 + 𝐶𝑠)

10𝐿 1ℎ𝑟

(

) (60min)

𝑉= ℎ

𝑚𝑜𝑙 𝑚𝑜𝑙

(13 𝐿 𝑚𝑖𝑛) (0.05 × 10 𝐿 )

10𝑚𝑜𝑙 0.5𝑚𝑜𝑙 0.03𝑚𝑜𝑙 0.5𝑚𝑜𝑙

( 𝐿 − 𝐿 )( + 𝐿 )

𝐿

VCSTR=0.1291 L

b)

𝐶𝑠𝑜 − 𝐶𝑠 𝑡

= −𝐾𝑚 + 𝑟𝑚𝑎𝑥 ( )

𝐶𝑠𝑜 𝐶𝑠

ln( 𝐶𝑠 ) ln (𝐶𝑠𝑜)

10 − 0.5 𝑡

= −(0.03) + (13) ( )

10 10

ln ( ) ln ( )

0.5 0.5

t = 0.7377 min

t=V/F

V=Ft

V=(0.7377 min)(1 h/ 60 min)(10 L/h)

VPFR = 0.1229 L

2.9 A substrate is decomposed in the presence of an enzyme according to the michaelis menten

equation with the following kinetic parameters:

grams

Km=10 liter

g

Rmax = 7 L−min

If we operate two 1-L CSTR n series at steady state, wht will be the concentration of substrate

leaving the second reactor? The flow rate is 0.5 L/min. The inlet substrate concentration is 50g/L

and the enzyme concentration in the two reactors is maintained in the sa value all of the time. Is

the two reactor system more efficient than one reactor whose volume is equal to the sum of the

two reactors?

GIVEN:

Cso

50g/L

Km= 10g/L

rmax= 7g/L-min

F= 0.5 L/min

REQUIRED:

a. Cs2

b. Is two reactor more efficient than 1 reactor with volume = 2L

rmax Csτ

Cs=-km + Cso−Cs

For the first reactor solve Cs1

7g 1l

( )(Cs2)( 0.5g )

L

min

Cs1= (-10g/L) + 50g

− Cs1

L

Cs1= 38.8650g/L

7g 1l

( )(Cs2)( 0.5g )

L

min

Cs2= (-10g/L) + 38.8650− Cs2

Cs2= 28.50120g/L

Cso−Cs

% conversion = x 100%

Cso

50−28.5012

%conversion = x 100%

50

7g 2l

( )(Cs2)( 0.5g )

L

min

Cs= (-10g/L) + 50g

− Cs1

L

50 − 29.1517

%conversion = x 100%

50

2.14 Eadie (1942) measured the initial reaction rate of hydrolysis of acetylcholine (substrate) by

dog serum (source of enzyme) in the absence and presence of prostigmine (inhibitor), 1.5 x 10-7

mol/L and obtained the following data:

Substrate Concentration Initial Reaction Rate Rate (mol/L.min)

(mol/L) Absence of Prostigmine Presence of Prostigmine

0.0032 0.111 0.059

0.0049 0.148 0.071

0.0062 0.143 0.091

0.0080 0.166 0.111

0.0095 0.200 0.125

b. Evaluate the Michaelis-Menten kinetic parameters in the presence of inhibitor by

employing the Langmuir plot.

0.09

0.08

y = 2.9883x + 0.0489

0.07

0.06

0.05 y = 3.3133x + 0.0191

Cs/r

0.04

0.03

0.02

0.01

0

0 0.001 0.002 0.003 0.004 0.005 0.006 0.007 0.008 0.009 0.01

Cs

b. Rmax= 1/m = 0.3346 (with inhibitor concentration)

Rmax= 1/m = 0.3018 (no inhibitor concentration)

Km = bRmax = 5.7644x10-3

KI = bRmax = 0.0164

CHAPTER 2: ENZYME KINETICS

2.17 The initital rate of reaction for the enzymatic cleavage of deoxyguanosine triphosphate was

measured as a function of initial substrate concentration as follows (Kornberg et al., J. Biol. Chem.,

233, 159, 1958):

Given:

Substrate Concentration Initial Reaction Rate

μmol/L μmol/L min

6.7 0.30

3.5 0.25

1.7 0.16

a. Calculate the Michaelis-Menten constants of the above reaction.

b. When the inhibitor was added, the initial reaction rate was decreased as follows:

Substrate Inhibitor Initial Reaction Rate

μmol/L Μmol/L Μmol/L min

6.7 146 0.11

3.5 146 0.08

1.7 146 0.06

Is this competitive inhibition or noncompetitive inhibition? Justify your answer by showing the

effect of the inhibitor graphically. [Contributed by Professor Gary F. Bennett, The university of

Toledo, Toledo, OH]

Required: MM constants

a) Langmuir a) Langmuir

𝐶𝑠 𝑘𝑚 1 𝐶𝑠 𝑘𝑚 1

= + (𝐶 ) = + (𝐶 )

𝑟 𝑟𝑚𝑎𝑥 𝑟𝑚𝑎𝑥 𝑠 𝑟 𝑟𝑚𝑎𝑥 𝑟𝑚𝑎𝑥 𝑠

r(max) = 0.4215 μmol/L-min r(max) = 0.1567 μmol/L-min

km = 3.6317 μmol/L km = 2.9807 μmol/L

b) Lineweaver Burk b) Lineweaver Burk

1 1 𝑘𝑚 1 1 1 𝑘𝑚 1 1

= + ( ) = + ( )

𝑟 𝑟𝑚𝑎𝑥 𝑟𝑚𝑎𝑥 𝐶𝑠 𝑟 𝑟𝑚𝑎𝑥 𝑟𝑚𝑎𝑥 𝐶𝑠

r(max) = 0.4511 μmol/L-min r(max) = 0.1416 μmol/L-min

km = 3.0566 μmol/L km = 2.3613 μmol/L

c) Eadie Hofstee c) Eadie Hofstee

𝑟 𝑟

𝑟 = 𝑟𝑚𝑎𝑥 + 𝑘𝑚 ( ) 𝑟 = 𝑟𝑚𝑎𝑥 + 𝑘𝑚 ( )

𝐶𝑠 𝐶𝑠

r(max) = 0.4336 μmol/L-min r(max) = 0.1457 μmol/L-min

km = 2.8096 μmol/L km = 2.5083 μmol/

Therefore, Langmuir isotherm best fit the data with r = 0.9968 for withoutinhibitor.

CHAPTER 2: ENZYME KINETICS

and L-tyrosine. It has been found (Frantz and Stephenson, J. Biol. Chem., 169, 359, 1947) that the

glutamic acid formed in the hydrolysis, inhibits (competitively) the progress of the reaction by

forming a complex with cathepsin. The course of the reaction is followed by adding tyrosine

decarboxylase which evolves CO2.

𝜇mole/mL 𝜇mole/mL 𝜇mole/mL.min

4.7 0 0.0434

4.7 7.57 0.0285

4.7 30.30 0.0133

10.8 0 0.0713

10.8 7.58 0.0512

10.8 30.30 0.0266

30.3 0 0.1111

30.3 7.58 0.0909

30.3 30.3 0.0581

Calculate (a) the value of Michaelis-Menten constants of the enzyme, Ks, and (b) the dissociation

constant of enzyme-inhibitor complex, KI.

600

y = 6.4106x + 329.1

500

R² = 0.9935

400

y = 6.5053x + 137.08

300 y =R²6.3732x

= 0.9986

+ 80.2

R² = 0.9993

200

100

0

0 5 10 15 20 25 30 35

a. @ I=0 @ I = 30.30

Rmax = 1/m = 0.1569 Rmax = 1/m = 0.1560

Ks = bRmax = 12.5839 KI = bRmax = 51.3368

@ I= 7.58

Rmax = 1/m = 0.1537

KI = bRmax = 21.0720

CHAPTER 2: ENZYME KINETICS ; ADDITIONAL PROBLEM

https://ww2.chemistry.gatech.edu/~lw26/bCourse_Information/3511/stud_comp/chap12_17.pdf

The following data were obtained for the reaction A ↔ B, catalyzed by the enzyme Aase. The

reaction volume was 1mL and the stock concentration of A was 5.0mM. Seven separate reactions

were examined, each containing a different amount of A. The reactions were initiated by adding

2.0µL of a 10µM solution of Aase. After 5 minutes, the amount of B was measured.

Reaction Volume of A Amount of B present

added(µL) at 5 minutes (nmoles)

1 8 26

2 10 29

3 15 39

4 20 43

5 40 56

6 60 62

7 100 71

(a) Calculate the initial velocity of each reaction (in units of µM.min-1)

(b) Determine the KM and Vmax of Aase from a Lineweaver-Burk plot.

(c) Calculate kcat.

SOL’N:

(a) νo = (26nmol/5min) / (1.0mL) x (103 mL/L) x (.001 µmol/1nmol) = 5.2 µM.min-1

Reaction νo(µM.min-1)

1 5.2

2 5.8

3 7.8

4 8.6

5 11.2

6 12.4

7 14.2

[A] = (.008mL)(5mM)(1mL) x (1000 µM/1 mM) = 40 µM

Reaction [S] µM (x) 1/[S] µM-1 ν(µM.min-1) (y) 1/ν (min-1/

µM)

1 40 0.025 5.2 0.192

2 50 0.02 5.8 0.172

3 75 0.0133 7.8 0.128

4 100 0.010 8.6 0.0116

5 200 0.005 11.2 0.089

6 300 0.0033 12.4 0.081

7 500 0.002 14.2 0.070

Vmax = 16 µM/min

x-int = -1/KM = 1/0.012

KM = 83 µM

(c) Calculate [E]T = (0.002mL)(10 µM Aase) / 1mL = 0.02 µM

Kcat = Vmax / [E]T = (16 µM/min) / 0.02 µM

Kcat= 800 /min

The statin drug lovastian helps lower cholesterol level by acts as competitive inhibitor on the

HMG-CoA reductase enzyme, which normally catalyzes an early step in the biosynthesis

pathway cholesterol

Required:

a) On a single graph, sketch the Michaelis-menten plot for HMG-CoA reductase in the presence

and absence of lovastatin, clearly labeling Km, and Vmax.

b) On a single graph, sketch the lineweaver-Burke (double reciprocal) plot for HMGCoA

reductase in the presence and absence of lovastatin. Clearly indicating how you could determin

Km, kcat and Vmax.

Solution:

a)

b)

Pesticide inhibition on enzyme has been reported, which caused the enzyme activity to reduce.

The collected data with and without inhibition are presented below. Determine the type of

inhibition and the KI for the inhibitor.

[S], M 3.30×10-4 5.00×10-4 6.70×10-4 1.65×10-3 2.21×10-3

Rate [I=0], 56 71 88 124 149

M/min×103

Rate

[I=20nM], 37 47 61 103 125

M/min×103

1 𝐾𝑚 1 1

Assuming Lineweaver-Burk Equation: =𝑉 +𝑉

𝑉 𝑚𝑎𝑥 𝑆 𝑚𝑎𝑥

1 𝐾𝑚

=5.0033×10-6 =4.3200×10-9

𝑉𝑚𝑎𝑥 𝑉𝑚𝑎𝑥

1

=5.1690×10-6

𝑉𝑚𝑎𝑥

𝐾𝑚 𝑎𝑝𝑝

=7.4605×10-9

𝑉𝑚𝑎𝑥

𝐾𝑚 𝑎𝑝𝑝 = 1.4433×10-3 M

𝐼 20×10−9 𝑀

𝐾𝑚 [1 + 𝐾 ] = 𝐾𝑚 𝑎𝑝𝑝 ; 8.6343×10-4 M [1 + ] =1.4433×10-3 M

𝐼 𝐾𝐼

𝐾𝐼 = 2.9780×10-8 M

𝐾𝐼 = 2.9780×10-8 M

CHAPTER 2: ENZYME KINETICS ; ADDITIONAL PROBLEM

A certain reaction has an activation energy of 125 kJ/mol. The rate is 0.33/s at 55ºC. Determine

the value of the specific rate constant at 100 ºC.

GIVEN: Ea=125 kJ/mol

@T1=55 ºC ; K55 ºC = 0.33

SOLUTION:

−𝐸𝑎

K =A𝑒 𝑅𝑇

@T1=55 ºC:

−125 𝑘𝐽/𝑚𝑜𝑙

8.314𝑘𝑗

(55+273)𝐾

0.33= A𝑒 𝑘𝑚𝑜𝑙.𝐾

A=2.6099×1019

@T2=100 ºC:

−125 kJ/mol

8.314kj

19 (100+273)K

K100ºC = (2.6099×10 )e kmol.K

K100ºC =82.8182/s

CHAPTER 2: ENZYME KINETICS ; ADDITIONAL PROBLEM

The enzyme carboxypeptidase catalyzes the hydrolysis of peptides. The following results were

obtained when the rate of enzymolysis of CBGP was monitored without inhibition at [CBGP]0=

0.713 mol/dm3.

𝐶𝐵𝐺𝑃 𝑚𝑜𝑙 1.25 3.84 5.81 7.13

,

10−2 𝑑𝑚3

𝑚𝑜𝑙 0.398 0.649 0.859 1.00

Rate, 𝑑𝑚3 .𝑠

When 2.0×10-3 mol/dm3 phenyl butyrate ion was added to the solution, the results were:

𝐶𝐵𝐺𝑃 𝑚𝑜𝑙 1.25 2.50 4.00 5.50

,

10−2 𝑑𝑚3

𝑚𝑜𝑙 0.172 0.301 0.344 0.548

Rate, 𝑑𝑚3 .𝑠

In a separate experiment, the effect of 5.0×10-2 mol/dm3 benzoate ion was monitored and the

results were:

𝐶𝐵𝐺𝑃 𝑚𝑜𝑙 1.75 2.50 5.00 10.00

,

10−2 𝑑𝑚3

𝑚𝑜𝑙 0.183 0.201 0.231 0.246

Rate, 𝑑𝑚3 .𝑠

Determine the type of inhibition and KI for phenyl butyrate and benzoate ion.

SOLUTION:

1 𝐾𝑚 1 1

Assuming Lineweaver-Burk Equation: =𝑉 +𝑉

𝑉 𝑚𝑎𝑥 𝑆 𝑚𝑎𝑥

y=0.8126+0.0216x

𝑉𝑚𝑎𝑥 = 1.2306 mol/dm3.s

𝐾𝑚 = 0.0266 mol/dm3

Line 2: with phenyl butyrate ion

y=1.0158+0.0601x

𝑉𝑚𝑎𝑥 = 0.9845 mol/dm3.s

𝐾𝑚 = 0.0592 mol/dm3

Line 3: with benzoate ion

y=3.7517+0.0300x

𝑉𝑚𝑎𝑥 = 0.2665 mol/dm3.s

𝐾𝑚 = 8.0228 mol/dm3

TYPE OF INHIBITION:

Phenyl Butyrate Ion: COMPETITIVE

Benzoate Ion: UNCOMPETITIVE

𝐼 2.0×10−3

𝐾𝑚 [1 + 𝐾 ] = 𝐾𝑚 𝑎𝑝𝑝 ; 0.0266 [1 + ] = 0.0592

𝐼 𝐾𝐼

𝐾𝐼 = 1.6369×10-3 mol/dm3

𝑉𝑚𝑎𝑥 1.2306

𝑉𝑚𝑎𝑥 𝑎𝑝𝑝 = 𝐼 ; 0.2665= 5.0×10−2

1+ 1+

𝐾𝐼 𝐾𝐼

𝐾𝐼 = 0.0138 mol/dm3

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