Questions on Enzymes: Assignment _26_03_24

1. What are enzymes, and what role do they play in biological systems?
ANSWER: Enzymes are proteins that speed up biochemical reactions in living
organisms by lowering the activation energy needed for the reactions to occur. They
are highly specific, catalyzing particular reactions, and play crucial roles in
metabolism, digestion, DNA replication, cell signaling, and other essential biological
processes.
2. How do enzymes catalyze chemical reactions?
ANSWER: Enzymes catalyze chemical reactions by binding to specific substrates,
lowering the activation energy required for the reaction to occur, facilitating the
conversion of substrates into products, and then releasing the products unchanged.
3. What factors can affect the activity of enzymes?
ANSWER: Factors affecting enzyme activity include temperature, pH, substrate
concentration, enzyme concentration, cofactors/coenzymes, inhibitors, activators, and
denaturation.
4. Can you explain the lock-and-key model and the induced fit model of
enzyme-substrate interaction?
ANSWER:

1. Lock-and-Key Model
- In the lock-and-key model, the enzyme's active site is considered rigid and
complementary in shape to the substrate, much like a key fits into a lock.
- According to this model, the substrate (the key) binds to the enzyme's active site
(the lock) with a precise fit, based on their specific shapes and chemical properties.
- The binding of the substrate to the active site induces the enzyme to undergo a
conformational change, facilitating the catalytic reaction.
- Once the reaction is complete, the products are released, and the enzyme returns to
its original conformation, ready to bind to another substrate molecule.

2. Induced Fit Model

 - The induced fit model proposes that the active site of the enzyme is flexible and
can undergo conformational changes upon substrate binding.
- In this model, the enzyme's active site initially has a shape that is complementary
but not perfectly matched to the substrate.
- When the substrate binds to the active site, both the enzyme and the substrate
undergo conformational changes to achieve a more precise fit.
- This induced conformational change brings reactive groups on the enzyme and
substrate into closer proximity, facilitating the catalytic reaction.
- As the reaction proceeds, the enzyme stabilizes the transition state of the reaction,
lowering the activation energy required for the conversion of substrate to product.
- After the reaction is complete, the products are released, and the enzyme returns to
its original conformation or may undergo further conformational changes.

5. What are some examples of enzymes and the reactions they catalyze?
ANSWER:

1. Amylase
- Catalyzes the hydrolysis of starch into smaller sugars such as maltose and glucose.

2. Lactase
- Catalyzes the hydrolysis of lactose (milk sugar) into its constituent
monosaccharides, glucose, and galactose.

3. Lipase
- Catalyzes the hydrolysis of lipids (fats) into fatty acids and glycerol.

4 Pepsin
- Catalyzes the hydrolysis of peptide bonds in proteins, breaking them down into
smaller peptides and amino acids. It is primarily active in the stomach.

5. DNA Polymerase
- Catalyzes the synthesis of new DNA strands by adding nucleotides to a growing
DNA chain during DNA replication.
 6. RNA Polymerase
- Catalyzes the synthesis of RNA molecules from DNA templates during
transcription.

6. How are enzymes classified based on their functions?

ANSWER: Enzymes can be classified based on their functions into six main categories:

1. Oxidoreductases :These enzymes catalyze oxidation-reduction reactions, involving the

transfer of electrons between molecules. Examples include dehydrogenases, which transfer
hydrogen atoms, and oxidases, which transfer oxygen atoms.

2. Transferases Transferases catalyze the transfer of functional groups, such as methyl, acetyl,
or phosphate gr:oups, between molecules. Examples include kinases, which transfer
phosphate groups, and transaminases, which transfer amino groups.

3. Hydrolases: Hydrolases catalyze hydrolysis reactions, where a molecule is cleaved by the

addition of water. Examples include lipases, which hydrolyze lipids, and proteases, which
hydrolyze peptide bonds in proteins.

4. Lyases: Lyases catalyze reactions where functional groups are added to or removed from a
molecule, without hydrolysis or oxidation. Examples include decarboxylases, which remove
carboxyl groups, and synthases, which catalyze the synthesis of new molecules.

5. Isomerases: Isomerases catalyze reactions that rearrange the atoms within a molecule,
converting it into its isomeric form. Examples include isomerases that catalyze the
conversion of glucose-6-phosphate to fructose-6-phosphate in glycolysis.

6. Ligases: Ligases, also known as synthetases, catalyze the joining of two molecules using
energy from ATP hydrolysis. These enzymes are involved in the synthesis of larger
molecules, such as DNA, RNA, and proteins.

7. What are enzyme inhibitors, and how do they affect enzyme activity?
ANSWER: Enzyme inhibitors are molecules that interfere with enzyme activity. Reversible
inhibitors include competitive, non-competitive, and uncompetitive inhibitors, while
irreversible inhibitors bind permanently to the enzyme. Competitive inhibitors compete with
the substrate for the active site, non-competitive inhibitors bind elsewhere on the enzyme,
and uncompetitive inhibitors bind to the enzyme-substrate complex. Irreversible inhibitors
form strong bonds with the enzyme, rendering it permanently inactive.
8. How do pH and temperature influence enzyme activity?
ANSWER: pH and temperature affect enzyme activity significantly. Enzymes have
an optimal pH at which they work best, and deviations from this pH can decrease
activity or denature the enzyme. Similarly, enzymes have an optimal temperature,
with activity increasing as temperature rises until denaturation occurs at excessively
high temperatures.
9. What are cofactors and coenzymes, and how do they assist enzymes in catalysis?
ANSWER: Cofactors and coenzymes are molecules that assist enzymes in catalyzing
biochemical reactions. Cofactors are inorganic ions or small organic molecules that directly
participate in catalysis, while coenzymes are small organic molecules that loosely bind to
enzymes and transfer chemical groups between molecules. They help enzymes by facilitating
substrate binding, stabilizing reaction intermediates, providing additional chemical
functionalities, and participating directly in chemical reactions.
10. Can you provide examples of industrial applications of enzymes?
ANSWER: Enzymes have numerous industrial applications:
1. Food industry: Enhance flavor, texture, and nutritional value.
2. Detergent industry: Aid in stain removal in laundry detergents.
3. Textile industry: Soften denim fabrics in denim processing.
4. Biofuel production: Convert biomass into biofuels.
5. Paper and pulp industry: Improve pulp bleaching and paper strength.
6. Pharmaceutical industry: Assist in synthesis and production of pharmaceuticals.
7. Wastewater treatment: Degrade organic pollutants in wastewater.
11. How are enzymes used in medical diagnostics and therapies?
ANSWER: Enzymes are pivotal in medical diagnostics and therapies. They're used in
diagnostic tests like ELISA and PCR to detect diseases. Enzyme replacement therapy
treats enzyme deficiencies, while enzyme inhibition therapy targets overactive
enzymes. Enzymes play roles in cancer treatment, drug metabolism, gene therapy, and
 biotechnology for drug production. Their specificity and efficiency make them
indispensable in modern medicine.
12. What role do enzymes play in digestion and nutrient absorption?
ANSWER: Enzymes play a critical role in digestion and nutrient absorption by
breaking down large molecules into smaller, absorbable forms. For instance:

1. Carbohydrate Digestion: Enzymes like amylase break down complex carbohydrates

into simpler sugars like glucose, facilitating absorption in the small intestine.

2. Protein Digestion: Proteases such as pepsin and trypsin break down proteins into
amino acids, which can be absorbed by the small intestine.

3. Fat Digestion: Lipases break down fats into fatty acids and glycerol, enabling
absorption through the small intestine.

4. Absorption Facilitation: Enzymes aid in breaking down nutrients into forms small
enough to be absorbed through the intestinal lining into the bloodstream for
distribution and utilization by the body.

13. How are enzymes involved in DNA replication and protein synthesis?
ANSWER: Enzymes play vital roles in both DNA replication and protein synthesis:

1. DNA Replication:
- DNA Polymerase: This enzyme synthesizes new DNA strands by adding
nucleotides complementary to the template strand during replication.
- Helicase: Unwinds the DNA double helix, separating the two strands to serve as
templates for replication.
- Primase: Synthesizes RNA primers that provide a starting point for DNA
polymerase to begin replication.
- Ligase: Seals the nicks in the sugar-phosphate backbone of the newly synthesized
DNA strands.

2. Protein Synthesis:
 - RNA Polymerase: Catalyzes the synthesis of mRNA by transcribing DNA
sequences into RNA molecules.
- Ribosomes: Ribosomal RNA (rRNA) and ribosomal proteins work together to
translate mRNA into proteins.
- Transfer RNA (tRNA): Carries specific amino acids to the ribosome, where they
are incorporated into the growing polypeptide chain.
- Aminoacyl-tRNA Synthetases: Enzymes that attach specific amino acids to their
corresponding tRNAs, ensuring accuracy in protein synthesis.

In short, enzymes facilitate DNA replication by synthesizing new DNA strands and
unwinding the double helix, while in protein synthesis, they are involved in
transcribing DNA into mRNA and translating mRNA into proteins.
14. What are some examples of genetic diseases caused by Enzymes catalyze chemical
reactions by binding to specific substrates, lowering the activation energy required for
the reaction to occur, facilitating the conversion of substrates into products, and then
releasing the products unchanged. deficiencies?
ANSWER: In short, some examples of genetic diseases caused by enzyme
deficiencies include:

1. Phenylketonuria (PKU): Deficiency in phenylalanine hydroxylase, leading to the

accumulation of phenylalanine and causing intellectual disabilities if untreated.

2. Gaucher's Disease: Deficiency in glucocerebrosidase, resulting in the accumulation

of glucocerebroside in cells, leading to organ enlargement and other complications.

3. Fabry Disease: Deficiency in alpha-galactosidase A, leading to the accumulation of

glycosphingolipids, causing kidney and heart problems.

4. Lactose Intolerance: Deficiency in lactase, leading to the inability to properly digest

lactose, causing gastrointestinal symptoms after consuming dairy products.

15. How do scientists study enzymes and their mechanisms of action?

ANSWER: In short, scientists study enzymes and their mechanisms of action through
various methods including:

- Biochemical Assays: These involve isolating enzymes and measuring their activity
under different conditions to understand their kinetics and substrate specificity.

- Structural Biology Techniques: X-ray crystallography, cryo-electron microscopy,

and nuclear magnetic resonance (NMR) spectroscopy reveal the three-dimensional
structures of enzymes, providing insights into their catalytic mechanisms.

- Genetic and Molecular Biology Techniques: Gene knockout, site-directed

mutagenesis, and recombinant DNA technology allow scientists to manipulate
enzyme genes and study their effects on enzyme function.

- Kinetic Analysis: Enzyme kinetics studies the rates of enzyme-catalyzed reactions,

providing information on enzyme-substrate interactions and reaction mechanisms.

- Computational Modeling: Molecular modeling and simulation techniques help

predict enzyme structures, dynamics, and interactions, aiding in the understanding of
enzyme mechanisms.