Oxidoreductases: Catalyze oxidation-reduction reactions

Transferases: Catalyze transfer of functional groups

Hydrolases: Catalyze hydrolysis reactions

Lyases: Catalyze addition or removal of groups to form double bonds

Isomerases: Catalyze isomerization reactions

Ligases: Catalyze joining of two molecules using ATP

Proteins consisting of long chains of amino acids

Three-dimensional structure critical for their function

Active site: Region where catalysis occurs

Co-factors: Non-protein molecules necessary for enzyme activity

Coenzymes: Organic co-factors

Substrate binds to the active site

Enzyme-substrate complex forms

Reaction occurs, transforming substrate to product

Product is released, enzyme is unchanged and can catalyze another reaction

Temperature: Optimum temperature for each enzyme

pH: Optimum pH for each enzyme

Substrate concentration: Enzyme activity increases with substrate concentration until saturation point

Enzyme concentration: Higher enzyme concentration leads to increased reaction rate

Cofactors and coenzymes: Required for proper enzyme function

Allosteric regulation: Molecules bind to regulatory sites, affecting enzyme activity

Enzyme inhibitors: Substances that reduce enzyme activity

Enzyme activation: Some enzymes are inactive until certain conditions or molecules activate them

Essential for metabolic processes in living organisms

Enable efficient chemical reactions at lower temperatures

Play a role in digestion, energy production, DNA replication, and many other biological processes

Used widely in industries such as food production and pharmaceuticals