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Chapter 9: Problem 114

Select the correct statement: (a) Increase in substrate concentration, increases the velocity of enzymatic reaction at first then it reaches maximum and further increment does not occur. (b) In competitive inhibition, the inhibitor closely resembles the substrate in its molecular structure. (c) Competitive inhibition are often used in the control of bacterial pathogens. (d) All of these

Short Answer

Expert verified
Therefore, the statement (d) 'All of these' is the correct answer as all the statements (a), (b), and (c) are accurate.

Step by step solution

01

Analyze statement (a)

Statement (a) is true. The rate of enzymatic reactions does increase with an increase in substrate concentration up to a certain point. After that point, (the maximum reaction velocity or Vmax), further increments in substrate concentration do not increase the rate of reaction because the enzymes are working at their maximum capacity and cannot process any more substrates.
02

Analyze statement (b)

Statement (b) is also true. In competitive inhibition, the inhibitor molecule closely resembles the substrate in its molecular structure and competes with the substrate for the active site on the enzyme. The inhibitor can bind to the active site, preventing the substrate from binding and slowing down the reaction.
03

Analyze statement (c)

Statement (c) is true as well. Competitive inhibitors are frequently used in the control of bacterial pathogens. Many drugs work by being competitive inhibitors and prevent the bacteria from carrying out necessary metabolic reactions.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Substrate Concentration
Enzymatic reactions are often influenced by the concentration of substrate, which is the substance an enzyme acts upon. At the beginning, increasing the substrate concentration usually speeds up the rate of the reaction. This is because more substrate molecules are available for the enzymes to act on. However, this increase in reaction speed does not continue indefinitely.
  • The reaction rate will increase until it reaches a point known as the maximum reaction velocity, or Vmax.
  • At Vmax, all the active sites of the enzyme molecules are occupied by substrate.
  • When this saturation point is reached, adding more substrate will not increase the reaction rate.
This is because the enzymes are already operating at full capacity. Understanding how substrate concentration affects enzyme activity is crucial for appreciating how biochemical reactions are regulated in different environments.
Competitive Inhibition
In the process of competitive inhibition, a molecule that resembles the enzyme's normal substrate binds to the enzyme's active site. This is the same location where the substrate binds during a standard enzymatic reaction.
  • The inhibitor molecule competes with the substrate for the active site.
  • This is only possible because the inhibitor strongly resembles the substrate in structure.
  • When the inhibitor binds to the active site, it prevents the substrate from binding and slows down the reaction.
The key to competitive inhibition is that it can be overcome by increasing the concentration of the substrate. At higher levels of substrate, the likelihood of the substrate binding to the enzyme rather than the inhibitor increases. This concept is important for understanding how to regulate enzymatic activity in a variety of settings, from biological processes to drug design.
Bacterial Pathogens Control
Controlling bacterial pathogens often involves inhibiting the metabolic pathways essential for their survival. Competitive inhibition is a common strategy used for this purpose.
  • Several drugs designed to control bacterial infections work by acting as competitive inhibitors.
  • These drugs target specific bacterial enzymes and prevent them from binding to their natural substrates.
  • This inhibition stops vital processes within the bacteria, ultimately saving the host from infection.
This approach is advantageous because it allows for specificity; the drug targets only bacterial enzymes, leaving human enzymes unaffected. Understanding competitive inhibition in this context helps in pharmaceutical development and the creation of antibiotics capable of combating resistant bacterial strains.

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Most popular questions from this chapter

Chemical analysis of living tissue (Vegetable or piece of liver \(+\mathrm{CCl}_{3} \mathrm{COOH}\) ) Acid soluble pool (Filterate) \(\quad\) Acid insoluble pool (retentate) 1\. mol. wt (a) 1\. It contain 4 type of organic compound a. Protein b. Polysaccharides C. d. Fill in the blanks in (1) and (2) in the above flowchart. (a) \(\mathrm{a} \rightarrow\) greater than 1000 Dalton \(\mathrm{b} \rightarrow\) Nucleotide (b) \(\mathrm{a} \rightarrow 18-800 \mathrm{Da}\) \(\mathrm{b} \rightarrow\) Nucleic acid (c) \(\mathrm{a} \rightarrow\) greater than \(10,000 \mathrm{Da}\) \(\mathrm{b} \rightarrow\) Oligosaccharides (d) \(\mathrm{a} \rightarrow\) greater than 1000 Dalton \(\mathrm{b} \rightarrow\) Nucleoside

Which one of the following are secondary metabolites? (a) Flavonoids and rubber (b) Antibiotics, coloured pigments and essential oils (c) Scents, gums, spices (d) All the above

Bond energy, which is stored in our body in the form of ATP is utilized in (a) Biosynthetic phase (b) Osmotic work (c) Mechanical work (d) All of these

Select the incorrect matching regarding the following diagram: (a) Purine Its metabolism forms uric acid (b) Uracil \(-\) It is exclusively found in RNA only (c) Adenylic acid \(-\) Monomer of both RNA and DNA (d) Cholesterol \(-\) Forms a part of cell membrane

Select the incorrect compounds that we get from living tissues can be called: (a) Elemental analysis of living tissues gives elemental composition of living tissue. (b) Analysis of chemical compound of living tissue gives idea of organic and inorganic constituent of living tissue. (c) Weight of small amount of living fresh tissue is known as wet weight. (d) Acid soluble pool contain lipids, nucleic acid, polysaccharide only.
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