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Molecule A is the substrate for enzyme X. Which is more likely to be a competitive inhibitor of enzyme X: molecule B or molecule C? Explain.

Short Answer

Expert verified

Molecule B is more likely to act as a competitive inhibitor of enzyme X because molecule B is structurally similar to the substrate (molecule A).

Step by step solution

01

Enzymes        

Enzymes are biological protein catalysts that change the rate of a process in a living organism. All the enzymes bear an active site which is the binding region of the substrates (reactant).

02

Competitive inhibitor

A competitive inhibitor is a chemical substance that competes with the substrate for the active site of the enzyme. Thus, a competitive inhibitor affects the rate of an enzyme-catalyzed reaction.

03

Molecule B act as a competitive inhibitor for enzyme X

Molecule A is Pyruvic acid.

Molecule B is Acetone.

Molecule C is 4-nitrophenyl acetate.

Molecules A and B are aliphatic, whereas molecule C is aromatic. Moreover, the structure of molecule B is identical to that of molecule A. This is because both molecules have three carbon atoms and a C=O group at the end of the chain.Thus, molecule B will act as a competitive inhibitor of enzyme X.

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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] (mMโปยน)

1/v0 (๐›Mโปยน.s)

0.5

2.4

1.0

2.6

1.5

2.9

2.0

3.1

Set B

1/[S] (mMโปยน)

1/v0(๐›Mโปยน.s)

8

5.9

10

6.8

12

7.8

14

8.7

What are the differences between instantaneous velocity, initial velocity, and maximal velocity for an enzymatic reaction?

List the factors that influence a drugโ€™s bioavailability.

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]

(๐›M)

vโ‚’ (mg minโปยน)

(no inhibitor)

vโ‚’ (mg minโปยน)

(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.

Why are uncompetitive and mixed inhibitors generally considered to be more effective in vivo than competitive inhibitors?

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