• All are globular proteins

• Act as a biologycal catalysts to increase the rate of biochemical reactions

•Do not change structurally and chemically after a reaction/reusable

• Highly specific for a particular substrate in a reaction

•Required in a small amount

• Lower the activation energy of a reaction by bringing the substrates into contact with one another

• May catalyse reversible or irreversible reactions

• Their activities are affected by pH, temperature, substrate concentration and enzyme concentration

•Their activities is maximum at optimum temperature/pH

• Can be denatured at extreme temperature or pH

• Enzyme possess active sites where the substrate molecules bind to for a reaction to take place

• Does not alter the nature of the end product of the reaction

•Catalyse the transfer of a functional group from one molecule to another

• Catalyse the rearrangement of functional group/ atoms within a substrate molecule by converting one isomer to another

•Catalyse certain reaction in which double bonds form or break

• Catalyse the reaction in which new chemical bonds are formed between the substrate molecule by using ATP as energy sources

• Change in the shape of enzyme's active site
•The enzyme changes its shape slightly
•The active site is flexible or not exactly complementary to the substrate
•Enzyme collides with substrate
•Substrate binds to the active site
•The binding induces a slight change in the active site of enzyme, allowing the substrate to fit to the enzyme precisely
•Active site become fully complementary with substrate to form enzyme-substrate (ES) complex
•Reaction takes place and converts the substrate to the product to form enzyme-product (EP) complex
•The shapes of enzyme and product do not complement, the product are released from its enzyme
• Active site of enzyme return back to original conformation
•Enzyme ready to bind with another substrate

•Catalyse the hydrolysis of substrate by the addition of water