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Enzyme X and enzyme Y catalyze the same reaction and exhibit the v0 versus [S] curves shown below. Which enzyme is more efficient at low [S]? Which is more efficient at high [S]?

Short Answer

Expert verified

Enzyme X will be more efficient when the substrate is high, and enzyme Y will be more efficient when substrate concentration is low.

Step by step solution

01

Enzymes

Enzymes are biological protein catalysts that change the rate at which a process occurs in a biological system. The substrate is a molecule that binds to the enzyme's substrate-binding site.

02

Comparison of Enzyme X and Enzyme Y

The sigmoidal curve of enzyme X is displayed, whereas the hyperbolic curve of enzyme Y is shown.Cooperative binding is represented by the sigmoidal curve, whereas the hyperbolic curve represents non-cooperative binding.

The enzyme X is more effective when the substrate concentration is high and exhibits cooperative binding. On the other hand, when the substrate concentration is low, the enzyme Y is more effective and exhibits non-cooperative binding.

Hence, enzyme X is more efficient when the substrate concentration is high, whereas enzyme Y is more efficient when the substrate concentration is low.

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Most popular questions from this chapter

Explain why each of the following data sets from a Lineweaver Burk plot are not individually ideal for determining KM for an enzyme catalysed reaction that follows Michaelis-Menten kinetics.

Set A

1/[S] (mM鈦宦)

1/v0 (饾泹惭鈦宦.蝉)

0.5

2.4

1.0

2.6

1.5

2.9

2.0

3.1

Set B

1/[S] (mM鈦宦)

1/v0(饾泹惭鈦宦.蝉)

8

5.9

10

6.8

12

7.8

14

8.7

The KM for the reaction chymotrypsin with N-acetylvaline ethyl ester is 8.8102M, and the KM for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6104M. (a) Which substrate has the higher apparent affinity for the enzyme? (b) Which substrate is likely to give a higher value for Vmax?

Sphingosine-1-phosphate (SIP) is important for cell survival. The synthesis of SIP from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below.

[Sphingosine]

(饾泹惭)

v鈧 (mg min鈦宦)

(no inhibitor)

v鈧 (mg min鈦宦)

(with threo-sphingosine)

2.5

32.3

8.5

3.5

40

11.5

5

50.8

14.6

10

72

25.4

20

87.7

43.9

50

115.4

70.8

Construct a Lineweaver-Burk plot to answer the following questions:

(a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor?

(b) What kind of an inhibitor is threo-sphingosine? Explain.

If there is 10 渭mol of the radioactive isotope 鲁虏P (half-life 14 days) at t=0, how much will 鲁虏P remain at (a) 7 days, (b) 14 days, (c) 21 days,
and (d) 70 days?

From the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant.

Time (s)

Reactant (mM)

0

5.4

1

4.6

2

3.9

3

3.2

4

2.7

5

2.3

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