A protein that functions as a biological catalyst - a substance that speeds up a chemical reaction without being changed by the reaction
Structure of enzymes
Contain up to 20 different amino acids linked together to form a chain which then folds into the globular enzyme shape
Have active sites which only match specific substrates
Lock and key model
Enzymes are folded into complex shapes that allow smaller molecules (substrates) to fit into them. The place where these molecules fit is called the active site.
Enzymes are highly specific - each type of enzyme can catalyse only one type of reaction (or just a few types of reactions)
Denaturation
Changing the shape of an enzyme's active site, for example because of high temperatures or extremes of pH. Denatured enzymes no longer work.
As temperature increases
The rate of an enzyme-catalysed reaction increases
At high temperatures
The rate of the enzyme-catalysed reaction decreases again because the enzyme becomes denatured and can no longer function as a biological catalyst
At low temperatures
The enzymes and substrates have low kinetic energy, resulting in fewer successful collisions between the substrate and the enzyme's active site
As temperature increases
The kinetic energy increases, leading to more collisions and enzyme substrate complexes formed per unit time, increasing the rate of reaction
At the optimum temperature
The maximum number of enzyme-substrate complexes form per unit time
If temperature continues to increase past the optimum
The increased kinetic energy breaks the weak hydrogen bonds holding the enzyme's unique active site shape, so enzyme–substrate complexes can no longer form as the substrates no longer fit into the active site
Optimum pH
The pH value at which an enzyme works best
Different enzymes work best at different pH values
The optimum pH for an enzyme depends on where it normally works
Intestinal enzymes have an optimum pH of about 7.5, but stomach enzymes have an optimum pH of about 2