Catalysts that speed up the rate of a chemical reactionwithout being changed or used up in the reaction
Proteins
Biological catalysts (biological because they are made in living cells, catalysts because they speed up the rate of chemical reactions without being changed)
Necessary to all living organisms as they maintain reaction speeds of all metabolic reactions (all the reactions that keep an organism alive) at a rate that can sustain life
Enzymes are specific to one particular substrate (molecule/s that get broken down or joined together in the reaction) as the enzyme is a complementary shape to the substrate
The product is made from the substrate(s) and is released
Enzyme specificity: lock and key model of enzyme activity
A) substrate
B) active site
C) enzyme-substrate complex
D) products
Enzymes are specific to one particular substrate(s) as the active site of the enzyme, where the substrate attaches, is a complementary shape to the substrate
This is because the enzyme is a protein and has a specific 3-D shape
This is known as the lock and key hypothesis
When the substrate moves into the enzyme’s active site they become known as the enzyme-substrate complex
After the reaction has occurred, the products leave the enzyme’s active site as they no longer fit it and it is free to take up another substrate
How enzymes work
Enzymes and substrates randomly move about in solution
When an enzyme and its complementary substrate randomly collide - with the substrate fitting into the active site of the enzyme - an enzyme-substrate complex forms, and the reaction occurs.
A product (or products) forms from the substrate(s) which are then released from the active site. The enzyme is unchanged and will go on to catalyse further reactions.
Enzymes are proteins and have a specific shape, held in place by bonds
This is extremely important around the active site area as the specific shape is what ensures the substrate will fit into the active site and enable the reaction to proceed
Enzymes work fastest at their optimum temperature
Heating to high temperatures beyond the optimum will break the enzyme's bonds and it will lose its shape - this denatures the enzyme
Substrates cannot fit into denatured enzymes as the shape of their active site has been lost
Denaturation is irreversible
Effect of temperature on enzyme activity
A) active site
B) amino acids
C) unique shape
D) amino acid chain
E) distorted
F) fits
G) high temperatures
H) forces
Increasing the temperature from 0⁰C to the optimum increases the activity of enzymes as the more energy the molecules have the faster they move and the number of collisions with the substrate molecules increases, leading to a faster rate of reaction
This means that low temperatures do not denature enzymes, they just make them work more slowly
Graph showing the effect of temperature on the rate of enzyme activity
If the pH is too high or too low, the bonds that hold the amino acid chain together to make up the protein can be destroyed
This will change the shape of the active site, so the substrate can no longer fit into it, reducing the rate of activity
Moving too far away from the optimum pH will cause the enzyme to denature and activity will stop
Graph showing the effect of pH on rate of activity for an enzyme from the duodenum