ENZYMES – Complete Study Guide

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

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