enzymes
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what are enzymes
biological catalysts that speed up chemical reactions in living cells by lowering the activation energy.
what is the general structure of enzymes
globular proteins with a unique three-dimensional shape. has an active site thats complementary to a specific substrate.
what does the lock and key model state
the active site fits the substrate perfectly and only 1 enzyme fits 1 type of substrate
what does the induced fit model state
the active site changes shape slightly to fit the substrate better when it binds. this makes the reaction more efficient
whats enzyme inhibition
when enzyme activity is slowed or stopped. it helps to regulate reactions.
what does a competitive inhibitor do
mimic the substrate and block the active site.
what does a non competitive inhibitor do
bind elsewhere and change the enzyme’s shape.
how is enzyme activity controlled
• inhibitors • temperature • ph levels • feedback mechanisms
how is temperature and ph important in controlling enzyme activity
enzymes have an optimum temp and ph, if they are too low / high the enzyme can can denature
what are feedback mechanisms
when the product binding to the enzyme turns it off when enough product has been made, it prevents waste and keeps the metabolism in balance
what 2 types of reaction do enzymes speed up
anabolic catabolic
what are anabolic reactions
where small molecules are built up into larger ones
what are catabolic reactions
where large molecules are broken down into smaller ones
what is the activation energy
the minimum amount of energy required for a chemical reaction to start
whats the velocity / rate of reaction
the speed a which a reaction occurs, how fast reactants are converted into products.
what are some factors that affect enzyme reaction time
• substrate concentration • enzyme concentration • temp • ph • inhibitors
what is reversible inhibition
includes both competitive and non competitive types inhibitor can dissociate from enzyme and enzyme return back to normal
what is irreversible inhibition
• inhibitor forms permanent covalent bond with the enzyme. • permanent inactivating
what is enzyme denaturing
when a protein looses its 3d structure due to breaking of bonds that maintains shape. the shape of the active site changes so the substrate can no longer bind to it.
how does breakdown of hydrogen bonds affect enzymes
hydrogen bonds maintain the enzymes tertiary structure. heat or ph can break these bonds which will result in the enzyme unfolding and becoming misshapen
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