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Mr Potter
Lesson Objectives
Enzyme unit overview
What are they?
How they work
Activation energy
What controls their activity
Rates of reaction
Substrate/enzyme concentrations
Temperature, pH
Enzyme inhibitors
Practical to demonstrate Catalase activity in different tissue
samples
Previous related topics covered?
Enzyme controlled reactions?
Proteins?
Lipase, protease, pectinase, amylase etc?
Lock & Key molecular structures?
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
Amylase + starch substrate
How do enzymes work?
Reaction Mechanism