Enzymes

Introduction
• Biologically active
• Tremendously increase rate of reaction
• Biological activity is restricted to a small portion called active site contain only few amino
acids
• Other structure is maintained by all other amino acids, allosteric site
• Structure is globular
• Non protein part is called cofactor essential for proper functioning contain mg+2, cu+2, fe+2,
zn+2 etc.
• Detachable cofactor is called coenzyme if it is inorganic
• Covalently attached is called prosthetic group
• Loosely attached is called coenzymes
• Enzyme with prosthetic group or coenzyme attached is called holoenzyme  Without
prosthetic group or coenzyme is called apoenzyme.

Characteristics

• Pepsin is very dangerous so it is released in inactive form pepsinogen

Structure
• All enzymes are globular proteins except riboenzyme
• Active site is divided into two functional site i.e. catalytic site and binding site
• Active site consists of 3-12 amino acids
• Catalytic site helps in formation of products of enzyme substrate complex
• Binding site helps in recognition of substrate and ES complex formation and activates
catalytic site.

Mechanism of Enzyme
 Enzyme has specific active site so it reacts with specific substances to form products from
them. They are very specific in their action.
 E+S ES complex E+P

 Emil Fischer proposed lock and key model in 1890

 Koshland proposed induced fit model in 1959
 Koshland model is more acceptable by scientists

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Factors Affecting Rate of Enzymes

1. Temperature
 Optimum temperature for humans is 37C.
 Every rise in 10C results in doubling the rate of reaction upto optimum
temperature.
 Rise in temperature more than optimum results in denaturing of enzymes.

2. pH
 Enzymes work in a narrow range of pH called optimum pH.
 A little change in pH can ionize an enzyme
 Ionization of enzymes happen due to pH
 In human, mostly enzymes work within pH range of 6 to 8 and other in acidic and
alkaline medium

Enzymes Optimum pH
Pepsin 2.00
Sucrase 4.50
Enterokinase 5.50
Salivary Amylase 6.80
Catalase 7.60
Chymotrypsin 7.00-8.00
Pancreatic lipase 6.80
Arginase 9.70

3. Concentration of Enzymes and Substrate

 Increase in concentration of enzymes and substrate increase the rate of reaction
but upto a limiting concentration.
 Rate of reaction is increased double by doubling the concentration of substrate
or enzymes. Reaction rate increases upto a certain limit because after a certain
increaser in concentration all active sites are occupied. So, further increase in
concentration doesn’t affect the rate.

Enzyme inhibitors
 Block the enzyme activity by occupying the active site
 Two types i.e. reversible and non-reversible
 Non-reversible inhibitors form covalent bond with active site and are not converted into
products
 Reversible inhibitors form weak bond with enzymes and their effect can be reversed by
increasing the concentration of substrate.

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  There are two types of reversible inhibitors i.e.
Competitive and non-competitive
 Competitive inhibitors form weak bonds with active site while non-competitive inhibitors
attach with allosteric site and thus changing the shape of enzymes.

Classification of Enzymes
 Enzymes are classified on the basis of their functions:

Type of Enzyme Work Example

Oxidoreductases Catalyze redox reaction by removing e or H ion Cytochrome oxidase
from substrate

Transferases Catalyze the transfer of specific functional Hexokinase, Glucokinase

group except H functional group

Hydrolases Catalyze the breakdown of large molecules Proteases, Lipases

into smaller by addition of water
molecules

Lyases Catalyze the breakdown of large molecules Histidine decarboxylase

into smaller without hydrolysis

Isomerases Forms isomers Phosphohexose

isomerase
Ligases Join together two molecules by utilizing energy DNA polymerases
RNA polymerases