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Assignment CH62

1. The decarboxylation of glyoxalate by mitochondria is inhibited by malonate in a competitive manner. The Km' is 1.26 mM and the KI is 1.95 mM. 2. Ionizing enzymes and substrates affect the rate of enzymatic reactions through changes in pH. 3. The biological oxidation of phenylacetic acid is inhibited by propionic acid in a mixed manner. The Km is 0.5 mM, Vmax is 2.5 mM/l-h, and KI is 1 mM.

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413 views

Assignment CH62

1. The decarboxylation of glyoxalate by mitochondria is inhibited by malonate in a competitive manner. The Km' is 1.26 mM and the KI is 1.95 mM. 2. Ionizing enzymes and substrates affect the rate of enzymatic reactions through changes in pH. 3. The biological oxidation of phenylacetic acid is inhibited by propionic acid in a mixed manner. The Km is 0.5 mM, Vmax is 2.5 mM/l-h, and KI is 1 mM.

Uploaded by

Swathi S
Copyright
© © All Rights Reserved
Available Formats
Download as PDF, TXT or read online on Scribd
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Please write this assignment in A4 sheets or blue book, submit soft copy by 30.03.2020.

Assessment will be based on soft copy. Hard copy can be submitted when you start attending
classes.

1) Decarboxylation of glyoxalate (S) by mitochondria is inhibited by malonate (I). The


following data was obtained in batch experiments:
Rate of CO2 Evolution, v (mmoles/l-h)

Glyox,S (mM) I=0 I = 1.26 mM I = 1.95 mM

0.25 1.02 0.73 0.56

0.33 1.39 0.87 0.75

0.40 1.67 1.09 0.85

0.50 1.89 1.30 1.00

0.60 2.08 1.41 1.28

0.75 2.44 1.82 1.39

1.00 2.50 2.17 1.82

a. What type of inhibition is this?


b. Determine the constants Vm, km’, and KI.

2) Explain effect of pH on enzyme catalyzed reaction. Derive an expression for rate of


reaction for ionising enzymes and ionising substrates.

3) Biological oxidation of phenylacetic acid is inhibited by propionic acid present in


wastewater. The following data were obtained for enzymatic oxidation of phenylacetic acid at
different concentrations of propionic acid:

S (mM) 0.25 0.40 0.50 0.60 0.75 1.00

V (mM/l-h), I = 0 1.0 1.7 1.9 2.1 2.4 2.5

V (mM/l-h), I = 1 mM 0.65 1.1 1.3 1.4 1.8 2.2

V (mM/l-h), I = 2 mM 0.55 0.9 1.0 1.3 1.4 1.8

a. What kind of inhibition is this?


b. Determine Vm, Km, and KI.
4) The hydration of is catalyzed by carbonic anhydrase as follows:

The following data were obtained for the forward and reverse reaction rates at pH 7.1 and an
enzyme concentration of 2.8 × 10–9 M:

Hydration Dehydration

1/v, M −1 (s × 10−3) [CO2] (M × 10−3) 1/v, M −1 (s × 10−3) (M ×103)

36 1.25 95 2

20 2.5 45 5

12 5 29 10

6 20 25 15

v is the initial reaction rate at the given substrate concentration. Calculate the forward and
reverse catalytic and Michaelis constants.

5) During a test of kinetics of an enzyme–catalyzed reaction, the following data were


recorded:

E0 (g/l) T (°C) I (mmol/ml) S (mmol/ml) V (mmol/ml-min)

1.6 30 0 0.1 2.63

1.6 30 0 0.033 1.92

1.6 30 0 0.02 1.47

1.6 30 0 0.01 0.96

1.6 30 0 0.005 0.56

1.6 49.6 0 0.1 5.13

1.6 49.6 0 0.033 3.70

1.6 49.6 0 0.01 1.89

1.6 49.6 0 0.0067 1.43


1.6 49.6 0 0.005 1.11

0.92 30 0 0.1 1.64

0.92 30 0 0.02 0.90

0.92 30 0 0.01 0.58

0.92 30 0.6 0.1 1.33

0.92 30 0.6 0.033 0.80

0.92 30 0.6 0.02 0.57

a. Determine the Michaelis–Menten constant for the reaction with no inhibitor present at
30°C and at 49.6°C.
b. Determine the maximum velocity of the uninhibited reaction at 30°C and an enzyme
concentration of 1.6 g/l.
c. Determine the KI for the inhibitor at 30°C and decide what type of inhibitor is being
used.

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