ENZYME =)

INTRODUCTION
Enzymes speed up chemical reactions without themselves being used up in the course of reaction. Enzymes are able to catalyse reactions in aqueous solutions under exceptionally mild conditions of temperature and pH.

 water-soluble globular proteins

complicated folding of the protein chain to form tertiary structure gives clefts which is the active site of the enzyme.
the active site is designed to fit a particular substrate molecules

The lock and key model

Complementary structures (enzyme specificity) only one substrate will fit into the active site. A reversible reactions. Providing alternative reaction pathway that requires lower activation energy, Ea

Energy profile for enzyme-catalysed and non-catalysed reactions

DENATURATION
Interactions with other chemical substances that cause irreversible changes in structure (loss of the correct structure and the destruction of enzyme activity) Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape.

Factor Affecting Enzyme Activity

Temperature
high temperature high kinetic energy Rate of enzyme activity increase Increase the frequency of collision greater proportion of the collisions involve molecules energy greater than activation energy > 40 C, disruption of the forces maintaining the shape of the molecules. Denatured (shape of active site change)

 pH
extremes of pH (high acidity or alkalinity) will denatured the proteins different enzymes will have different pH optimum

 Chemical denaturation
high salt concentration will cause denaturation (disrupting ionic interactions between different region of the chain) Urea denatures protein by disrupting the hydrogen bonds (that maintain the secondary and tertiary structure of the protein) The effect are reversible

COMPETITIVE INHIBITOR
Competitive inhibitor molecules that have a similar shape to the substrate molecule. The molecules can bind to the active site. No reaction take place, the correct substrate cannot attach to the enzyme. This inhibition is reversible by an increase in a substrate concentration.

NON-COMPETITIVE INHIBITOR
Non-competitive inhibitor molecules can bind on to regions of the enzyme other than the active site Affect the enzyme activity It binds to the enzyme, preventing the catalysed reaction from occurring but it does not bind to the active site. But the binding can cause : the active site change shape Enzyme-substrate complex change shape

 It binds weakly to the enzyme. It is reversible when the conc of inhibitor falls, the enzyme-substrate complex fall apart, the functional shape of the enzyme is restored.