Enzymatic Function of Proteins

enzymes are very specific, usually catalyzing only one type of chemical reaction or a small group of related reactions

enzymes alone without their cofactors are termed apoenzymes, while the complete active forms are called holoenzymes

cofactors or coenzymes firmly attached and essential for an ezyme’s activity are called prosthetic groups

cofactors are typically inorganic substances that usually include metal ions or minerals

coenzymes are cofactors made up of organic molecules often derived from vitamins

temperatures higher than 37 degrees C cause enzyme activity to decline due to denaturation

enzymes operate at an optimal pH, which aligns with the enzyme’s environment, reflecting the enzyme’s adaptiation to its specific biological function

high salinity or osmolarity can disrupt the H and ionic bonds that maintain an enzyme’s 3-D structure, leading to denaturation or a change in the enzyme’s shape and its ability to bind to its substrate efficiently

lyases: enzymes that catalyze the breaking of chemical bonds

isomerases: catalyze the rearrangement of atoms within a molecule, leading to the formation of isomeric forms

ligases: catalyze the joining of two molecules

hydrolases: catalyze the cleavage of chemical bonds through the addition of water

oxioreductases: catalyze redox reactions, which involve the transfer of electrons between molecules

transferases: catalyze the transfer of functional groups from one molecule to another

reversible inhibition: involves inhibitors that bind to enzymes in a non-covalent manner

competitive inhibition: binds to the substrate’s active site

non-competitive inhibition: inhibitor binds to a site other than the active site, often called an allosteric site, and reduce’s the enzymes catalytic efficiency

uncompetitive inhibition: binding occurs at an allosteric site, not at the active site, effectively locking the substrate within the complex and preventing the reaction from proceeding to product formation