INTRODUCTION
What are enzymes?
- All living organisms (plants, animals, microorganisms) need energy to perform life activities
- Life activities include: Growth → Development → Locomotion
- This energy comes from food through the process of metabolism
METABOLISM
Definition: All the chemical reactions which are done inside the cell
Two Types of Metabolism:
1. CATABOLISM
- Complex → Simple
- Example: Respiration
2. ANABOLISM
- Simple → Complex
- Example: Photosynthesis
NOTE: Enzymes speed up or accelerate these chemical reactions for life activities
ENZYME DEFINITION
Enzyme: Biological catalyst which speed up or accelerate chemical reaction inside the living system
Etymology (Word Origin)
- Greek word: “Put available”
- En- means = Inside
- Zyme means = Yeast
- This name is based on discovery
DISCOVERY OF ENZYMES
Historical Timeline:
1833 – Anselme Payen:
- First time discovered enzyme in the process of diastases
- Starch → Glucose conversion
Louis Pasteur (Bacteriologist):
- During fermentation: Sugar → Alcohol
- This process occurs with the help of yeast
- Yeast (vital forces are present) ↓
- Ferment (enzyme)
NOTE: First time discovered by Louis Pasteur
1877 – Kuhne:
- The name ferment was converted into enzyme
1897 – Buchner:
- Enzyme was first extracted from zymase
STRUCTURE OF ENZYMES
Two Main Parts:
1. ALLOSTERIC SITE
- Largest part
- Gives shape to enzyme
2. ACTIVE SITE
- Functional part
- Three dimensional
- Smallest part
- Every enzyme has specific active site
- Enzymes are specific in nature
- Contains 2-12 amino acid charge
Components of Active Site:
A. BINDING SITE
- Attachment of substrate
- Recognition of substrate
B. CATALYTIC SITE
- It provides energy to activate substrate during reaction
CHARACTERISTICS OF ENZYMES
1. Biological Catalyst
- Speed up chemical reaction in living system
2. Chemical Nature
- All enzymes are protein in nature
- Mostly tertiary protein
- Exception: Ribozyme
3. Specific in Function
- Each enzyme is specific
- Specific function means specific enzyme speed up specific chemical reaction
- Because of specific active site
Examples:
- Carbohydrate digestion → Amylase
- Protein digestion → Pepsin
- Lipid digestion → Lipase
4. Used in Less Amount
- Enzymes are used in less amount during chemical reaction
Example: A + B → C + D
5. Remain Unchanged
- Enzymes are not used during chemical reaction
- E + S → ES → E + P
- Enzyme + Substrate → Enzyme-Substrate complex → Enzyme + Product
6. Reduce Activation Energy
- Enzyme reduces activation energy during chemical reaction
Definitions:
- Activation Energy: Energy required to start a chemical reaction
MODE OF ENZYME ACTION
How enzymes speed up a reaction:
General Reaction:
Without enzyme: A + B → C + D (30 minutes) With enzyme: A + B → C + D (3 minutes)
Reasons for Speed:
1. Reduce Activation Energy
- In chemical reaction for the formation of new substance
- Old bond break → New bond form
Example: H₂O + O₂ → H₂O
- H—H + O → O
- Old bond + Reduce energy → New bond form
- Break → Energy → Form
Rate of chemical reaction:
- Without enzyme: R → P (30 min)
- With enzyme: R → P (3 min)
2. More Active Sites
- Each enzyme has more than 1000s of active sites
Chemical Reaction:
- Without enzyme: Complete in 30 minutes
- With enzyme: Complete in 3 minutes
NOTE: Different models explain the mode of enzyme action:
- Lock and Key Model
- Induced Fit Model
- These models explain the activity of an enzyme
LOCK AND KEY MODEL
Background:
- This model was presented by Emil Fischer in 1890
- Shows relationship between active site and substrate
Key Points:
- Active site is complementary to substrate
- Like lock and key mechanism
- Substrate fits perfectly into active site
- Forms enzyme-substrate complex
- Products are released
- Enzyme remains unchanged
FACTORS AFFECTING ENZYME ACTIVITY
1. TEMPERATURE
Low Temperature (Below 30°C)
- At this temperature the bonds are very condensed
- At 30°C enzyme are inactive
- Small amount substrate cannot fit exactly
- At 30°C enzyme become non-specific
High Temperature (Above 40°C)
Types:
- High: Substrate → Product
- Optimum: At 40°C the bond becomes flexible and enzyme denatures
- At 30°C the rate of reaction increases
- At 40°C the enzyme becomes non-specific
Optimum Temperature (37°C)
- Rate of reaction is maximum
- S—P (Substrate to Product conversion)
2. pH (Power of Hydrogen Ion)
For Normal Function of Enzyme:
- Need specific pH
- At this pH enzyme shows maximum work
- Any fluctuation in normal function of enzyme will affect
Reason:
- All enzymes are globular proteins and are sensitive to pH
Types:
High pH (Above 8)
- When pH = 8
- More OH ion → S → P
- Enzyme inactive
Optimum pH
- Enzyme: Pepsin in stomach pH 1
- s = P5
Low pH (Below 5)
- When pH = 5, Pepsin in stomach
- More H ion → S → P
- Enzyme inactive
3. SUBSTRATE CONCENTRATION
- Higher substrate concentration increases enzyme activity up to saturation point
4. ENZYME CONCENTRATION
- More enzymes mean faster reaction rate up to a limit
SUMMARY
- Enzymes are biological catalysts made of proteins
- They speed up chemical reactions by lowering activation energy
- Have specific active sites for specific substrates
- Work best at optimum temperature (37°C) and pH
- Follow Lock and Key or Induced Fit models
- Essential for all metabolic processes in living organisms