Are 3-d proteins, have many different types with each one having its own specific substrate, are reactants, are organic catalysts, are reused, lower activation energy
How they work
Lower the Ea (enzyme activation energy) without changing the enzyme itself
Higher reaction rates
Reaction rates are 10^6 to 10^12 times faster than uncatalyzed reactions
Milder conditions
Work at temps less than 100 degrees Celsius, atmospheric pressure, neutral pH
Greater reaction specificity
Lock and key theory
Capacity for regulation
Enzymatic activity can be controlled easily. Y the concentration of other substances (inhibition)
Non protein enzymes made from vitamins that help out enzyme reactions
active site
The part of an enzyme or antibody where the chemical reaction occurs, works because stress is placed on bonds, ionic bonding interaction with substrate, R groups/ acidic/basic, covalent bonds
Enzyme available with empty active site, substrate bonds to enzyme with induced fit, substrate is converted to products, products are released
Activation energy
Energy that is needed to get a reaction started
Non competitive inhibitor
binds to a site on the enzyme that is not the active site, the allosteric site, important in cell metabolism, helps in negative feedback, may be reversible ex: too much sucrose
Competitive inhibitors
bind to the active site of an enzyme, competing with the substrate ex: toxins, poisons, certain chemicals