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Enzymes
Mr Potter
Lesson Objectives
Enzyme unit overview
What are they? How they work
Activation energy
samples
By the end of the unit you should be able to: Explain enzymes as Globular Proteins which act as catalysts Explain their catalytic action in terms of lowering activation energy Describe examples of enzyme-catalysed reactions Discuss factors affecting reaction rates and inhibition Describe how to investigate these effects experimentally
Enzymes:
Are defined as a BIOLOGICAL catalyst i.e. something that speeds up a reaction. Up to 1012 fold
Usually end in ase. Discovered in 1900 in yeasts. Some 40,000 in human cells Control almost every metabolic reaction in living organisms Are globular proteins coiled into a very precise 3-dimentional shape with hydrophilic side chains making them soluble Possess an active site such as a cleft in the molecule onto which other substrate molecules can bind to form an enzyme-substrate complex Once the substrate has been either synthesised or split, enzymes can be re-
used.
Do not create reactions Widely used in industrial cleaning Often require co-factors (co-enzymes) to function metal ions, or vitamin derivatives
Molecule Geometry
Substrate molecule fits into the enzyme like a lock & key. Enzyme shape distorts or it changes other factors to make the reaction happen
Activation Energy
In a natural reaction the product has a lower energy than the substrate so equilibrium will take it in the direction of the product. However there is an energy barrier to be overcome Enzymes lower the activation energy required to bring about a reaction. EG catalase reduces the activation energy for the reduction of H202 86-fold