Temperature
Enzymes in humans usually have an optimum temperature of 37.5° C
As temperature increases, enzyme activity increases
Increasing temperature makes the enzyme and substrate particles vibrate faster, making it more likely for collisions to occur between the active site and the substrate
Temperatures above the optimum begin to break the bonds between the amino acids that the enzyme is made of
As the bonds break, the shape of the active site changes so it no longer fits the substrate, denaturing the enzyme
pH
The pH scale measures from 0 (acidic) to 14 (alkaline)
Deviation from the optimum pH begins to denature the enzyme, as with temperature
Enzymes can tolerate small changes in pH, but if the change is too large the damage is irreversible
Substrate Concentration
Large amounts of substrate can trigger/activate enzymes
As substrate concentration increases, reaction rate increases until all active sites are occupied. This is called the saturation point
Enzyme Concentration
The concentration of enzyme affects how much substrate can be acted upon
Increasing enzyme concentration does not always result in a greater rate of enzyme activity, as enzymes are not used up during reactions
Presence of Salt
Ions in the salt can interfere with the intermolecular forces between enzymes
Enzyme Inhibitors
Enzyme inhibitors compete with the substrate for the active site. There are two types of inhibitors:
Competitive - Occupies the active site so that the substrate cannot bind to it
Non-competitive - Binds to some other part of the enzyme, making it harder for the substrate to bind to the active site but not stopping it completely
Cofactors & Coenzymes
Sometimes, cofactors and coenzymes are needed in order for an enzyme to catalyse a reaction
Cofactors - Bind permanently to an enzyme, increasing the speed of the reaction. They are metal ions, such as K+ and Zn2+
Coenzymes - Carry chemical groups between enzymes, loosely binding to them. They are organic molecules, such as Biotin and Vitamin B