Class 11 : Biology (In English) – Lesson 9. Biomolecules
EXPLANATION & SUMMARY
πΏβ¨ Introduction
π§ Biomolecules are organic compounds produced by living organisms that form the building blocks of life.
They include carbohydrates, proteins, lipids, nucleic acids, and metabolites essential for growth, structure, and metabolism.
πΏ Every living cell is a chemical factory performing numerous reactions simultaneously using these biomolecules.
Without them, life processes like energy production, genetic transmission, and structural formation are impossible.
π‘ Concept:
Life is chemical; cell = chemical system.
Understanding biomolecules explains how life functions at molecular level.
𧬠Types of Biomolecules

Living organisms contain inorganic (water, salts, minerals) and organic (carbohydrates, lipids, proteins, nucleic acids) compounds.
1οΈβ£ Inorganic Biomolecules
π§ Water β universal solvent; ~70% of cell weight
π§ Minerals β NaβΊ, KβΊ, CaΒ²βΊ, MgΒ²βΊ, phosphate, essential for enzymes, structure, and osmoregulation
2οΈβ£ Organic Biomolecules
π§ Contain carbon; form complex macromolecules performing structural and functional roles.
πΎ Carbohydrates
π§ Definition: Organic compounds with C, H, O, generally Cβ(HβO)β
π‘ Called saccharides; primary energy source.

π§© Classification
π¬ 1. Monosaccharides
Simple sugars, 1 unit
Examples: Glucose, Fructose, Galactose
Soluble, sweet, energy-rich

π 2. Disaccharides
2 monosaccharides linked by glycosidic bond
Examples: Sucrose (glucose + fructose), Maltose (glucose + glucose), Lactose (glucose + galactose)

π 3. Polysaccharides
Long chains of monosaccharides
Storage: Starch (plants), Glycogen (animals)
Structural: Cellulose (plants), Chitin (arthropods)
βοΈ Note: Hydrolysis of polysaccharides yields simple sugars.
π‘ Concept:
Carbohydrates = instant energy source (4 kcal/g).

π§ Lipids
π§ Definition: Heterogeneous group of compounds like fats, oils, waxes, insoluble in water but soluble in organic solvents.
βοΈ Functions:
Energy storage (9 kcal/g)
Structural (cell membranes = phospholipids)
Protective (cuticle, insulation)
Hormonal precursors (steroids)

π§ͺ Types
1οΈβ£ Simple lipids β esters of fatty acids + glycerol (triglycerides)
2οΈβ£ Compound lipids β with other groups (phospholipids, glycolipids)
3οΈβ£ Derived lipids β steroids (cholesterol), fat-soluble vitamins
πΏ Fatty acids:
Saturated β single bonds (butter)
Unsaturated β double bonds (oils)
π‘ Concept: Lipids store 2.5Γ more energy than carbohydrates.
𧬠Proteins
π§ Definition: Complex macromolecules of amino acids linked by peptide bonds.
π§ͺ Elements: C, H, O, N (sometimes S, P)
π§± Structure
1οΈβ£ Primary: linear chain of amino acids
2οΈβ£ Secondary: Ξ±-helix or Ξ²-sheet (H-bonds)
3οΈβ£ Tertiary: 3D folding (functional shape)
4οΈβ£ Quaternary: multiple polypeptides (e.g., haemoglobin)

π§ Functions
𧬠Enzymatic β catalyse reactions (amylase)
πͺ Structural β keratin, collagen
βοΈ Transport β haemoglobin
π§« Defense β antibodies
π‘ Regulatory β hormones (insulin)
π Energy source during starvation
βοΈ Note: ~20 amino acids form all proteins.
π‘ Concept: Proteins = βworkhorsesβ of the cell.
π§« Nucleic Acids
π§ Definition: Polymers of nucleotides; store and transmit genetic information.
π§© Nucleotide = nitrogen base + sugar + phosphate
πΏ Types

𧬠DNA (Deoxyribonucleic acid)
Double helix (Watson & Crick model)
Sugar: deoxyribose
Bases: A, T, G, C
Base pairing: AβT (2 H-bonds), GβC (3 H-bonds)
Function: genetic code, heredity
π‘ RNA (Ribonucleic acid)
Single-stranded
Sugar: ribose
Bases: A, U, G, C
Types: mRNA, tRNA, rRNA
Function: protein synthesis
π‘ Concept:
DNA = blueprint; RNA = messenger & worker.
π§ͺ Enzymes
π§ Definition: Biological catalysts made of proteins, speed up reactions without being consumed.
βοΈ Properties:
Specific to substrate
Function under optimum pH and temperature
Reusable
Inhibited by poisons
π§© Mechanism
𧬠Lock and Key Model β substrate fits enzyme
π§ͺ Induced Fit Model β enzyme adjusts to substrate
π‘ Example: Amylase converts starch β maltose.

π§ͺ Metabolites
πΏ 1. Primary Metabolites
π§ Found in all cells; essential for life
π§ Examples: amino acids, sugars, nucleotides

πΈ 2. Secondary Metabolites
πΏ Specific to species; not essential but useful
βοΈ Examples: alkaloids (morphine), pigments, essential oils
βοΈ Note: Secondary metabolites have medicinal, ecological value.

π§ Analysis of Chemical Composition
π§ͺ Living tissue analysis reveals 98% weight from:
C, H, O, N, P, S, Ca, Mg, K, Na, Cl
βοΈ About 5000+ compounds found in cells.
πΏ Bonds in Biomolecules

Covalent bonds β strong, stable (CβC, peptide)
Hydrogen bonds β weak, stabilise DNA, proteins
Ionic bonds β between charged groups

Glycosidic β carbohydrate link

Ester bond β lipid formation
Peptide bond β amino acids linkage

π‘ Concept: Bonds determine structure and function.
π Why This Lesson Matters
πΏ Connects chemistry and biology
𧬠Explains molecular basis of life processes
π§ Builds foundation for biochemistry and genetics
β‘ Vital for NEET, CBSE, and research fields
π Quick Recap
π§ͺ Biomolecules: organic + inorganic compounds
π Carbohydrates: energy source (mono, di, poly)
π§ Lipids: energy storage, structure, insulation
πͺ Proteins: amino acid polymers; functional molecules
𧬠Nucleic acids: DNA (genetic), RNA (protein synthesis)
βοΈ Enzymes: biological catalysts
πΈ Metabolites: primary (essential), secondary (specialised)
π Summary
All living cells contain a variety of biomolecules that form the chemical basis of life.
Carbohydrates provide energy, lipids store energy and form membranes, proteins perform structural and functional roles, and nucleic acids carry genetic information.
Enzymes catalyse biochemical reactions, ensuring life runs efficiently.
These molecules interact to sustain metabolism, growth, and reproduction.
Studying biomolecules bridges chemistry and biology, revealing how simple molecules create the complexity of living systems.
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QUESTIONS FROM TEXTBOOK
π΅ Question 1. What are macromolecules? Give examples.
π’ Answer:
𧬠Macromolecules are large, complex molecules formed by the polymerization of smaller units called monomers. They have high molecular weight and are essential for the structure and function of cells.
πΏ Examples:
β‘οΈ Polysaccharides (e.g., starch, glycogen)
β‘οΈ Proteins (e.g., enzymes, collagen)
β‘οΈ Nucleic acids (DNA, RNA)
β‘οΈ Lipids (though not always polymeric, some are macromolecular in size)
βοΈ Function: Structural, catalytic, genetic, and energy storage roles.
π΅ Question 2. What is meant by tertiary structure of proteins?
π’ Answer:
π§« The tertiary structure is the three-dimensional folding of a protein chain resulting from interactions among amino acid side chains.
πΏ Types of bonds responsible:
β‘οΈ Hydrogen bonds
β‘οΈ Ionic bonds
β‘οΈ Disulfide bridges
β‘οΈ Hydrophobic interactions
π‘ This structure determines the functional shape of a protein (globular or fibrous).
βοΈ Example: Enzymes like pepsin and hemoglobin.
π΅ Question 3. Find and write down structures of 10 interesting small molecular weight biomolecules. Find if there is any industry which manufactures the compounds by isolation. Find out who are the buyers.
π’ Answer:
πΈ Examples of small molecular weight biomolecules:
Glucose
Fructose
Ribose
Glycerol
Amino acids (glycine, alanine)
Fatty acids
Nucleotides
Urea
Cholesterol
Lactic acid
π Industries: Pharmaceutical, food, and cosmetic industries isolate these molecules.
π Buyers: Research laboratories, hospitals, food industries, cosmetic companies.
βοΈ Purpose: Used in medicines, nutrition, and biochemical research.
π΅ Question 4. Find out and make a list of proteins used as therapeutic agents. Find other applications of proteins (e.g., Cosmetics etc.)
π’ Answer:
𧬠Proteins as therapeutic agents:
β‘οΈ Insulin: Diabetes treatment
β‘οΈ Interferons: Antiviral, anticancer
β‘οΈ Monoclonal antibodies: Cancer therapy
β‘οΈ Albumin: Maintains osmotic pressure in patients
β‘οΈ Thrombin/Fibrinogen: Blood clotting
π Other applications:
Collagen: Cosmetics, anti-aging creams
Keratin: Hair products
Casein: Nutritional supplements
βοΈ Significance: Proteins play key roles in medicine and industry.
π΅ Question 5. Explain the composition of triglyceride.
π’ Answer:
βοΈ Triglyceride = 1 molecule of glycerol + 3 molecules of fatty acids.
Each fatty acid is linked to glycerol by ester bonds.
π§ Formula:
Glycerol (CβHβ
(OH)β) + 3 Fatty acids β Triglyceride + 3HβO
βοΈ Function: Major form of energy storage in animals and plants.
π΅ Question 6. Can you attempt building models of biomolecules using commercially available atomic models (Ball and Stick models)?
π’ Answer:
πΏ Yes, Ball and Stick models help visualize the 3D arrangement of atoms and bonds in biomolecules.
π‘ Students can model glucose, amino acids, nucleotides, fatty acids to understand spatial orientation.
βοΈ Useful in studying molecular geometry and bond angles.
π΅ Question 7. Draw the structure of the amino acid, alanine.
π’ Answer:
π§« Structure of Alanine (CβHβNOβ):
Central Ξ±-carbon bonded to:
β‘οΈ Amino group (-NHβ)
β‘οΈ Carboxyl group (-COOH)
β‘οΈ Hydrogen atom
β‘οΈ Methyl group (-CHβ)
βοΈ Diagram description:
H
|
H2NβCβCOOH
|
CH3
βοΈ Alanine is a non-polar, aliphatic amino acid.
π΅ Question 8. What are gums made of? Is Fevicol different?
π’ Answer:
πΏ Gums are polysaccharides (complex carbohydrates) secreted by plants for protection.
β‘οΈ Examples: Gum arabic, guar gum, tragacanth.
π§ͺ Fevicol is synthetic, made of polyvinyl acetate (PVA), not a natural polysaccharide.
βοΈ Hence, Fevicol is different from natural gums.
π΅ Question 9. Find out a qualitative test for proteins, fats and oils, amino acids and test any fruit juice, saliva, sweat and urine for them.
π’ Answer:
π§« Tests:
Proteins: Biuret test (violet color)
Fats and oils: Sudan III test (red color)
Amino acids: Ninhydrin test (blue-violet color)
π‘ Application: Test biological samples like saliva, fruit juice, urine for presence of biomolecules.
π΅ Question 10. Find out how much cellulose is made by all the plants in the biosphere and compare it with how much paper is manufactured by man and hence what is the consumption of plant material by man annually. What a loss of vegetation!
π’ Answer:
π± Plants produce ~ 10ΒΉΒΉβ10ΒΉΒ² tonnes of cellulose annually (largest organic compound on Earth).
π Paper industry consumes millions of tonnes annually, leading to deforestation.
π‘ Impact: Loss of vegetation, biodiversity, ecological imbalance.
βοΈ Promotes need for sustainable practices and recycling.
π΅ Question 11. Describe the important properties of enzymes.
π’ Answer:
𧬠Enzymes are biological catalysts made of proteins (or RNA).
πΏ Properties:
Catalytic efficiency β increase reaction rate.
Specificity β act on specific substrates.
Optimum conditions β best at specific pH and temperature.
Reversibility β can catalyse both forward and backward reactions.
Saturation β rate increases with substrate concentration up to a limit.
Denaturation β lose activity at high temperature or extreme pH.
βοΈ Conclusion: Enzymes regulate all metabolic reactions in living cells.
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OTHER IMPORTANT QUESTIONS FOR EXAMS
(CBSE MODEL QUESTIONS PAPER)
ESPECIALLY MADE FROM THIS LESSON ONLY
π΄ Question 1:
Biomolecules are primarily composed of:
π΄1οΈβ£ C, H, O, N
π’2οΈβ£ Na, K, Mg, Ca
π‘3οΈβ£ Fe, Cu, Zn, Co
π΅4οΈβ£ P, S, Cl, F
π’ Answer: 1οΈβ£ C, H, O, N
π΄ Question 2:
Which of the following is a monosaccharide?
π΄1οΈβ£ Sucrose
π’2οΈβ£ Glucose
π‘3οΈβ£ Maltose
π΅4οΈβ£ Lactose
π’ Answer: 2οΈβ£ Glucose
π΄ Question 3:
The simplest carbohydrate is:
π΄1οΈβ£ Sucrose
π’2οΈβ£ Fructose
π‘3οΈβ£ Glucose
π΅4οΈβ£ Monosaccharide
π’ Answer: 4οΈβ£ Monosaccharide
π΄ Question 4:
Which of the following is a disaccharide?
π΄1οΈβ£ Glucose
π’2οΈβ£ Sucrose
π‘3οΈβ£ Starch
π΅4οΈβ£ Cellulose
π’ Answer: 2οΈβ£ Sucrose
π΄ Question 5:
The storage polysaccharide in plants πΏ is:
π΄1οΈβ£ Glycogen
π’2οΈβ£ Starch
π‘3οΈβ£ Cellulose
π΅4οΈβ£ Chitin
π’ Answer: 2οΈβ£ Starch
π΄ Question 6:
The storage polysaccharide in animals πΎ is:
π΄1οΈβ£ Starch
π’2οΈβ£ Cellulose
π‘3οΈβ£ Glycogen
π΅4οΈβ£ Fructose
π’ Answer: 3οΈβ£ Glycogen
π΄ Question 7:
Proteins are polymers of:
π΄1οΈβ£ Sugars
π’2οΈβ£ Fatty acids
π‘3οΈβ£ Amino acids
π΅4οΈβ£ Nucleotides
π’ Answer: 3οΈβ£ Amino acids
π΄ Question 8:
The basic structural unit of nucleic acids is:
π΄1οΈβ£ Nucleotide
π’2οΈβ£ Ribose
π‘3οΈβ£ Nitrogen base
π΅4οΈβ£ Deoxyribose
π’ Answer: 1οΈβ£ Nucleotide
π΄ Question 9:
Which one is a purine base?
π΄1οΈβ£ Adenine
π’2οΈβ£ Thymine
π‘3οΈβ£ Cytosine
π΅4οΈβ£ Uracil
π’ Answer: 1οΈβ£ Adenine
π΄ Question 10:
Which vitamin is fat soluble?
π΄1οΈβ£ Vitamin C
π’2οΈβ£ Vitamin B
π‘3οΈβ£ Vitamin D
π΅4οΈβ£ Vitamin H
π’ Answer: 3οΈβ£ Vitamin D
π΄ Question 11:
Name the two types of nucleic acids found in living organisms.
π’ Answer:
1οΈβ£ DNA (Deoxyribonucleic acid): Genetic material in most organisms.
2οΈβ£ RNA (Ribonucleic acid): Involved in protein synthesis.
π΄ Question 12:
Define metabolites and name their types.
π’ Answer:
Definition: Molecules present in cells involved in metabolism.
Types:
β1οΈβ£ Primary metabolites: Essential for life (e.g. amino acids, sugars).
β2οΈβ£ Secondary metabolites: Non-essential, specialised roles (e.g. alkaloids, pigments).
π΄ Question 13:
What are carbohydrates? Write their classification with examples.
π’ Answer:
Definition: Organic compounds made of C, H, O in ratio 1:2:1; main energy source.
Classification:
β1οΈβ£ Monosaccharides: Single sugar unit; e.g. Glucose, Fructose.
β2οΈβ£ Disaccharides: Two monosaccharides; e.g. Sucrose (Glucose + Fructose).
β3οΈβ£ Polysaccharides: Many sugar units; e.g. Starch, Glycogen, Cellulose.
π‘ Function: Provide energy, structural support.
π΄ Question 14:
What are lipids? Mention their functions.
π’ Answer:
Definition: Organic compounds made of C, H, O; insoluble in water but soluble in organic solvents.
Examples: Fats, oils, phospholipids, steroids, waxes.
Functions:
β1οΈβ£ Energy storage (twice that of carbohydrates).
β2οΈβ£ Component of cell membrane (phospholipids).
β3οΈβ£ Insulation and protection.
β4οΈβ£ Hormone formation (steroids).
π΄ Question 15:
What are proteins? Describe their structure and functions.
π’ Answer:
Definition: Polymers of amino acids linked by peptide bonds.
Structure:
β1οΈβ£ Primary: Sequence of amino acids.
β2οΈβ£ Secondary: Coiling (Ξ±-helix) or folding (Ξ²-sheet).
β3οΈβ£ Tertiary: 3D structure.
β4οΈβ£ Quaternary: Two or more polypeptides.
Functions:
ββοΈ Structural (collagen),
ββοΈ Enzymatic (amylase),
ββοΈ Transport (haemoglobin),
ββοΈ Defence (antibodies).
π΄ Question 16:
What are nucleic acids? Write their components and types.
π’ Answer:
Definition: Macromolecules carrying genetic information.
Components:
β1οΈβ£ Nitrogen base: Purines (A, G), Pyrimidines (T, C, U).
β2οΈβ£ Pentose sugar: Ribose / Deoxyribose.
β3οΈβ£ Phosphate group.
Types:
β1οΈβ£ DNA: Genetic material in most organisms.
β2οΈβ£ RNA: Helps in protein synthesis.
π΄ Question 17:
Write differences between DNA and RNA.
π’ Answer:
Feature DNA RNA
Sugar Deoxyribose Ribose
Bases A, T, G, C A, U, G, C
Strand Double-stranded Single-stranded
Function Genetic material Protein synthesis
π΄ Question 18:
What are enzymes? Mention their properties.
π’ Answer:
Definition: Biocatalysts made of protein, speed up reactions.
Properties:
β1οΈβ£ Specific in action.
β2οΈβ£ Required in small amounts.
β3οΈβ£ Highly efficient.
β4οΈβ£ Affected by temperature, pH.
β5οΈβ£ Not consumed in reaction.
Example: Amylase, Lipase.
π΄ Question 19:
What are co-factors? Mention their types.
π’ Answer:
Definition: Non-protein components required by enzymes for activity.
Types:
β1οΈβ£ Prosthetic group: Tightly bound (e.g. FAD).
β2οΈβ£ Coenzyme: Loosely bound organic molecules (e.g. NADβΊ, CoA).
β3οΈβ£ Metal ions: Inorganic activators (e.g. MgΒ²βΊ, ZnΒ²βΊ).
π‘ Enzyme + Co-factor = Holoenzyme.
π΄ Question 20:
Write a note on primary and secondary metabolites.
π’ Answer:
Primary metabolites:
ββοΈ Essential for normal metabolism.
ββοΈ Examples: Carbohydrates, proteins, lipids, nucleic acids.
Secondary metabolites:
ββοΈ Non-essential; specialised functions (defence, pigments).
ββοΈ Examples: Alkaloids, flavonoids, rubber, essential oils.
π΄ Question 21:
What is a peptide bond? How is it formed?
π’ Answer:
Definition: Covalent bond joining two amino acids.
Formation:
ββ’ Between carboxyl group (-COOH) of one amino acid and amino group (-NHβ) of another.
ββ’ Involves removal of water (condensation reaction).
Example: Formation of dipeptide from two amino acids.
π΄ Question 22:
What is denaturation of proteins?
π’ Answer:
Definition: Loss of native structure of protein without breaking peptide bonds.
Causes: Heat, pH change, chemicals.
Result: Loss of biological activity.
Example: White of egg (albumin) becomes solid on boiling.
π΄ Question 23:
Describe the structure of an amino acid and explain the different types of amino acids.
π’ Answer:
Structure:
βEach amino acid consists of β
ββ1οΈβ£ Amino group (-NHβ)
ββ2οΈβ£ Carboxyl group (-COOH)
ββ3οΈβ£ Hydrogen atom (H)
ββ4οΈβ£ Side chain (R group) attached to Ξ±-carbon.
βπ§ͺ General formula: NHββCH(R)βCOOH
Classification (based on R group):
β1οΈβ£ Non-polar: Glycine, Alanine.
β2οΈβ£ Polar uncharged: Serine, Threonine.
β3οΈβ£ Acidic: Aspartic acid, Glutamic acid.
β4οΈβ£ Basic: Lysine, Arginine.
β5οΈβ£ Aromatic: Phenylalanine, Tyrosine.
π‘ Function: Building blocks of proteins; structural and enzymatic roles.
π΄ Question 24:
Explain the structure and functions of enzymes.
π’ Answer:
Structure:
β1οΈβ£ Globular proteins with active sites.
β2οΈβ£ Apoenzyme (protein part) + Cofactor = Holoenzyme (active form).
β3οΈβ£ Active site: Region binding substrate forming enzyme-substrate complex.
Functions:
ββοΈ Lower activation energy.
ββοΈ Catalyse metabolic reactions (digestion, respiration).
ββοΈ Highly specific to substrate.
ββοΈ Can be reused; work at optimum temperature & pH.
π‘ Examples:
ββ’ Amylase β converts starch β maltose.
ββ’ Lipase β converts lipids β fatty acids & glycerol.
π΄ Question 25:
Explain enzyme action mechanism (Lock and Key model).
π’ Answer:
Proposed by: Emil Fischer (1894).
Concept:
β1οΈβ£ Enzymeβs active site fits substrate specifically like a key fits a lock.
β2οΈβ£ Forms enzyme-substrate complex.
β3οΈβ£ Reaction occurs β product formed.
β4οΈβ£ Enzyme released unchanged.
π§ Equation:
βE + S β ES β E + P
Feature: Explains specificity; enzyme reusable.
π΄ Question 26:
Describe the structure of DNA.
π’ Answer:
Proposed by: Watson and Crick (1953).
Structure:
β1οΈβ£ Double helix of two polynucleotide chains.
β2οΈβ£ Backbone: Sugar (deoxyribose) + phosphate.
β3οΈβ£ Bases: Adenine (A), Thymine (T), Guanine (G), Cytosine (C).
β4οΈβ£ Base pairing: A = T (2 H-bonds), G β‘ C (3 H-bonds).
β5οΈβ£ Antiparallel strands: 5’β3′ and 3’β5′.
β6οΈβ£ One turn = 10 base pairs (distance 3.4 nm).
π‘ Function: Genetic material; stores hereditary information.
π΄ Question 27:
Explain the structure of RNA and its types.
π’ Answer:
Structure:
β1οΈβ£ Single-stranded polynucleotide chain.
β2οΈβ£ Sugar: Ribose.
β3οΈβ£ Bases: A, G, C, U (uracil replaces thymine).
Types:
β1οΈβ£ mRNA: Carries genetic code from DNA to ribosome.
β2οΈβ£ tRNA: Brings amino acids for protein synthesis.
β3οΈβ£ rRNA: Structural component of ribosomes.
π‘ Function: Involved in protein synthesis.
π΄ Question 28:
Discuss the factors affecting enzyme activity.
π’ Answer:
1οΈβ£ Temperature:
ββ’ Activity increases with temperature till optimum (~37Β°C).
ββ’ High temperature β denaturation.
2οΈβ£ pH:
ββ’ Each enzyme has optimum pH (e.g. Pepsin β pH 2).
3οΈβ£ Substrate concentration:
ββ’ Increases activity till saturation.
4οΈβ£ Enzyme concentration:
ββ’ Directly proportional to rate (if substrate excess).
5οΈβ£ Cofactors presence:
ββ’ Required for maximum activity.
π΄ Question 29:
What are cofactors? Describe their types with examples.
π’ Answer:
Definition: Non-protein components helping enzyme action.
Types:
β1οΈβ£ Prosthetic group: Tightly bound, e.g. FAD in succinate dehydrogenase.
β2οΈβ£ Coenzyme: Loosely attached organic molecules, e.g. NADβΊ, CoA.
β3οΈβ£ Metal ions: Inorganic activators, e.g. MgΒ²βΊ, ZnΒ²βΊ.
π‘ Holoenzyme = Apoenzyme + Cofactor
π΄ Question 30:
Explain metabolic pathways with an example.
π’ Answer:
Definition: Series of enzyme-mediated reactions in a cell.
Example: Glycolysis
β1οΈβ£ Glucose β Glucose-6-phosphate
β2οΈβ£ β Fructose-1,6-bisphosphate
β3οΈβ£ β Pyruvic acid
Each step catalysed by a specific enzyme.
Significance: Converts substrates into useful products, releases energy.
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