What are Enzymes?

Enzymes are substances that act as a catalyst in various chemical and biochemical reactions occurring inside our body. Enzymes are generally categorized as proteins, the only exception to this generalisation is the presence of catalytic RNA. Enzymes works or catalyse a biochemical reaction by lowering the activation energy barrier of the reaction. It is important to understand that enzymes do not change the chemical equilibrium of the reaction and is not consumed during the process. Enzymes work by adhering to reactant molecules and maintaining them in a position that allows chemical bond-breaking and bond-forming to occur more easily. The article provides MCQs on enzymes for a comprehensive understanding of the topic. These questions will help students in the preparation of various competitive examinations. 

 

Multiple Choice questions on Enzymes

Since we have revised the basic details of the enzymes, let us look into the MCQs of enzymes which are specifically aimed to develop a precise understanding of the concept. 

 

1. The general mechanism is that an enzyme acts by:

  1. Reducing the activation energy

  2. Increasing activation energy

  3. Decreasing pH value

  4. Increasing the pH value

Answer: Reducing the activation energy

Explanation: Enzymes catalyse the biochemical reactions by participating as a catalyst they are simply responsible for increasing the rate of reaction. Enzymes catalyse a reaction by binding substrate to the active site and various non-covalent interactions are formed and broken which provides energy. This energy from bond formation and breakage counteracts the activation barrier thus lowering the activation energy. 

 

2. The coenzyme is:

  1. Often a metal

  2. always a protein

  3. often a vitamin

  4. always an inorganic compound

Answer: Often a vitamin

Explanation: Coenzymes are chemical molecules that are required for catalytic activity by numerous enzymes. Vitamins or vitamin compounds are often used. In the absence of enzymes, they can operate as catalysts, although not as effective as when used in combination with an enzyme. 5-Deoxyadenosylcobalamin (coenzyme B12), flavin adenine dinucleotide, and lipoate are examples of common coenzymes.

 

3. An enzyme that joins the ends of two strands of nucleic acid is:

  1. Polymerase

  2. ligase

  3. synthetase

  4. Helicase

Answer: Ligase

Explanation: DNA ligase is the enzyme responsible for the formation of the phosphodiester bond between nucleotide base pairs.  This enzyme plays an important role in the DNA damage repair pathways.  

 

4. Which of the following is produced with the combination of apoenzyme and coenzyme:

  1. Holoenzyme

  2. Enzyme substrate complex

  3. Prosthetic group

  4. Enzyme product complex

Answer: Holoenzyme

Explanation: Holoenzymes are catalytically active enzymes that are coupled with cofactor or prosthetic groups, according to the definition of biochemistry. The apoenzyme is the protein portion of the enzyme that does not include the prosthetic group.

 

5. Which one among them is the example of competitive inhibition of an enzyme:

  1. Succinic dehydrogenase by malonic acid

  2. Cytochrome oxidase by cyanide

  3. Hexokinase by glucose-6-phosphate

  4. Carbonic anhydrase by carbon dioxide

Answer: Succinic dehydrogenase by malonic acid

Explanation:  The inhibition of succinic dehydrogenase by malonic acid is an example of the competitive inhibition of an enzyme. A competitive inhibitor looks like the substrate and binds to the enzyme's active site. The substrate is then barred from binding to the same active site as the enzyme. Malonate is a competitive inhibitor of succinate dehydrogenase: it binds to the enzyme's active sites without reacting, and therefore competes with succinate, the enzyme's regular substrate.

 

6. Blocking of enzyme action by blocking its active site is called as:

  1. Allosteric inhibition

  2. Feedback inhibition

  3. Competitive inhibition

  4.  Non-competitive inhibition

Answer: Competitive inhibition

Explanation: Competitive inhibitors are structural analogues of the substrate and hence compete for the same active binding sites on the enzyme as the substrate. Because of this rivalry, the impact of the competitive inhibitor can be overcome if enough substrate is given, i.e., the substrate will eventually fill all binding sites.

 

7. Diastase takes part in digestion of which one:

  1. Protein

  2. Starch

  3. Amino acids

  4. Fat

Answer: Starch

Explanation: Any of set of enzymes that catalyse the breakdown of starch into maltose is known as diastase. Urine diastase is effective in detecting ambiguous abdominal situations, particularly when pancreatitis, stones in the common bile duct, jaundice, and ruling out postoperative pancreatic damage are suspected; provided the diastase level is associated with clinical symptoms of the patient.

 

8. Enzyme catalysing rearrangement of atomic grouping without altering molecular weight or number of atom is:

  1.  Ligase

  2.  Isomerase

  3.  Oxidoreductase

  4.  Hydrolase

Answer: Isomerase

Explanation: Isomerases are enzymes that aid in the conversion of a chemical substance from one isomeric form to another by catalysing isomerization modifications in a molecule. Isomerization is the process of converting one isomer into another. Any of two or more versions of a molecule having the same chemical formula but a distinct stereochemical arrangement of the atoms is referred to as an isomer.

 

9. Enzyme complex involved in alcoholic fermentation is:

  1. Zymase

  2. Invertase

  3. Lipase

  4. Amylase

Answer: Zymase

Explanation: Zymase is a complex of enzymes that catalyses the conversion of sugar to ethanol and carbon dioxide. It's found in yeasts naturally. The activity of zymase differs amongst yeast strains.

 

10. Zymogen or proenzyme is a :

  1. Modulator

  2. Vitamin

  3. Enzyme precursor

  4. Hormone

Answer: Enzyme precursor

Explanation: Enzyme precursors are the inactive form of the enzymes which are generally activated by action of another enzyme or chemical compounds, the activation of such enzymes are highly regulated by the cell signalling pathways. 

 

11. Enzymes are made Up of:

  1. Fats

  2. Proteins

  3. Nucleic acids

  4. Vitamins

Answer: Proteins

Explanation: The enzymes are the tertiary and quaternary structures of the protein, the only exception to it is the presence of the catalytic RNA molecules.

 

12. Enzymes are polymers of:

  1. Hexose sugar

  2. Amino acids

  3. Fatty acids

  4. Inorganic phosphate

Answer: Amino acid

Explanation: Enzymes are mostly proteins, proteins are defined as the polymers of amino acids thus enzymes can be defined as the polymer of the amino acids.  

 

13. The enzyme which hydrolyses starch to maltose is:

  1. Protease

  2. Amylase

  3. Lactase

  4. Maltase

Answer: Amylase

Explanation: Amylases are a family of starch-hydrolyzing enzymes. Many enzymes work with starch or oligosaccharides made from it. Hydrolases such as -amylase, -amylase, glucoamylase, -glucosidase, debranching enzymes, and transferases such as CGTase, 4--glucanotransferase, and a branching enzyme are among the 19 enzymes recognised as belonging to the microbial amylase group. 

 

14. This enzyme was first isolated and purified in the form of crystals:

  1. Urease

  2. pepsin

  3. Amylase

  4. Ribonuclease

Answer: Urease

Explanation: Urease is a cytosolic enzyme that catalyses the conversion of urea to ammonia and CO2. Ureases are members of the amidohydrolases and phosphotriesterases superfamily. Ureases may be found in a wide variety of bacteria, fungi, algae, plants, and animals, as well as in soils as a soil enzyme. They are high-molecular-weight nickel-containing metalloenzymes.

 

15. This statement about enzymes is true:

  1. Enzymes accelerate reactions by lowering the activation energy

  2. Enzymes are proteins whose three-dimensional form is key to their function

  3. Enzymes do not alter the overall change in free energy for a reaction

  4. All of these

Answer: All of these

Explanation: Enzymes catalyze the biochemical reaction, they increase the rate of reaction by lowering the activation barrier. They are generally tertiary and quaternary proteins, they are not consumed in the reaction.

 

16. Koshland proposed which model:

  1. Fluid mosaic model

  2. Induced fit model

  3. Lock and key model

  4. Reflective index model

Answer: Induced fit model

Explanation: The induced fit model is a model for the interaction of enzymes and substrates. It states that only the appropriate substrate may cause the active site to align properly, allowing the enzyme to fulfil its catalytic job. It also implies that the active site changes until it is entirely attached to the substrate, at which time the final shape and charge are decided.

 

17. In the human body optimum temperature for enzymatic activities is:

  1. 37-degree celsius

  2. 25-degree celsius

  3. 20-degree celsius

  4. 15-degree celsius

Answer: 37 degrees celsius

Explanation: Enzymes are temperature sensitive, they tend to denature in high temperatures, the optimal temperature for the enzymes in the human body is around 37 degrees celsius.

 

18. Optimum pH value of pepsin is:

  1. 1.4

  2. 2

  3. 3.5

  4. 5

Answer: 1.4

Explanation: pH plays an important role in enzyme activity, enzymes are often active only in a narrow pH range. Pepsin gets denatured in pH lower and higher than the pH range of 1.4 to 1.6. The optimal pH for pepsin activity is 1.4.

 

19. The enzyme minus its coenzyme known as:

  1. Apoenzyme

  2. Metalloenzyme

  3. Isoenzyme

  4. All of these

Answer: Apoenzyme

Explanation: The apoenzyme is the protein part of the holoenzyme. Apoenzymes and prosthetic groups combinely to form the holoenzymes. 

 

20. Which of the following is the non-protein component of the enzyme?

  1. Cofactor

  2. Activator

  3. Coenzyme

  4. All of these

Answer: All of these

Explanation: Cofactor and coenzymes are the parts of the holoenzyme. Holoenzyme is the catalytic complex that contains both the protein part of an enzyme known as apoprotein and the metal-organic and organic compounds, that is cofactor and coenzymes. 

 

21. An uncatalyzed reaction involved:

  1. High activation energy

  2. Low activation energy

  3. Balanced activation energy

  4. All of these

Answer: High activation energy

Explanation: The high activation energy required for the catalysis of the biochemical reaction is a major barrier of the uncatalyzed reaction in the cells.

 

22. Which among them is not attribute of enzymes:

  1. Specific in nature

  2. Protein in chemistry

  3. Consumed in reaction

  4. Increased rate of reaction

Answer: Consumed in reaction

Explanation: The enzymes only lower the activation barrier of the biochemical reaction, they do not change the equilibrium, the enzyme also does not get consumed in the reaction. 

 

23. Zn +2 is an inorganic activator for enzymes:

  1. Carbonic anhydrase

  2. Phosphatase

  3. Chymotrypsin

  4. Maltase

Answer: Chymotrypsin

Explanation: The zinc cation is a cofactor of the enzyme chymotrypsin it is required for enzyme catalysis.

 

24. Mg +2 is an inorganic activator for enzymes:

  1. Phosphatase

  2. Carbonic anhydrase

  3. Amylase

  4. Enterokinase

Answer: Phosphatase

Explanation: Mg ions (cation) acts as cofactor of the enzyme phosphatase that is required for the enzyme activity. 

 

25. Which among them is a cofactor:

  1. Inorganic ion

  2. Organic molecule

  3. Both A and B

  4. None of these

Answer: Both A and B 

Explanation: A cofactor is an apoprotein that has a metal ion or one or more inorganic ions linked to it. Mg2+, Fe2+, Zn2+, and Mn2+ are examples of common cofactors. Metallic cofactors are used by enzyme examples including Cytochrome oxidase, catalase, peroxidase, pyruvate kinase, hexokinase, and glucose 6-phosphatase.

In conclusion of the article, we have discussed multiple questions that will help in understanding the enzyme.

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