Enzyme unit overview
What are they?
How they work
What controls their activity
Rates of reaction
Practical to demonstrate “Catalase” activity in different tissue samples
Enzyme controlled reactions?
Lipase, protease, pectinase, amylase etc?
“Lock & Key” molecular structures?
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
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
In any chemical reaction a substrate is converted into a product.
In an enzyme catalysed reaction the substrate first binds to the active site of the enzyme to form the enzyme-substrate complex
Substrate molecule fits into the enzyme like a lock & key.