Oxidoreductases - catalyze oxidation-reduction reactions.
Transferases - transfer functional groups between molecules.
Hydrolases - catalyze the hydrolysis of various bonds.
Lyases - break bonds by means other than hydrolysis and oxidation.
Isomerases - facilitate the rearrangement of atoms within a molecule.
Ligases - join two molecules together using ATP.
Temperature and pH - each enzyme has an optimal temperature and pH at which it is most active.
Substrate concentration - increasing substrate concentration increases the rate of reaction to a point of saturation.
Inhibitors - molecules that decrease enzyme activity. These can be competitive, non-competitive, or uncompetitive.
Activators - molecules that increase enzyme activity.
Medical - used in diagnostics, disease treatment, and as drug targets.
Industrial - employed in food processing, biofuel production, and waste management.
Biotechnology - used in genetic engineering, protein engineering, and the development of biosensors.
Allosteric regulation - where molecules bind to sites other than the active site to modulate activity.
Feedback inhibition - where the end product of a metabolic pathway inhibits an enzyme involved earlier in the pathway.
Covalent modification - such as phosphorylation, which can activate or deactivate enzymes.
Stability - enzymes can be sensitive to environmental changes and may denature outside their optimal conditions.
Purification - isolating enzymes from complex biological mixtures can be difficult and time-consuming.
Specificity and Sensitivity - designing assays that accurately measure enzyme activity without interference can be challenging.
