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define enzyme
biological catalysts that increase the rate of reaction and are not chemically altered in the process. made out of globular proteins
properties of enzymes
globular proteins
specific due to conformation at active site
effective in small amounts
remain chemically unchanged at the end of reaction
lowers activation energy of reaction
extremely efficient
biological catalysts
definition of activation energy
energy required to make substances react
why are enzymes helpful in terms of activation energy
the larger the activation energy, the slower the reaction
enzymes lower activation energy which makes reaction faster
what are the two hypotheses used to describe enzyme action
LOCK AND KEY HYPOTHESIS
INDUCED FIT HYPOTHESIS
describe the lock and key hypothesis
active site has a specific shape to which the substrate binds
substrate (key) is complementary to and fits exactly into shape of active site (lock) which forms an enzyme-substrate complex
once reaction is completed, the products no longer fit into active site and are released. active site is now free to receive new substrates
describe the induced fit hypothesis
some enzymes and their active sites are physically flexible
shape of substrate complementary to active site but not exact fit
binding of substrate to active site induces a small conformational change in enzyme shape
enables substrate to fit more snugly in the active site, forming enzyme-substrate complex
once reaction is completed, the products no longer fit into active site and are released. active site is now free to receive new substrates
how enzymes work
substrate and enzyme collide at correct orientation
substrate binds to enzyme at active site, forming a short-lived enzyme-substrate complex.
chances of reaction occuring is greatly enhanced
reaction occurs
once reaction is completed, the products no longer fit into active site and are released. active site is now free to receive new substrates. enzyme is chemically unchanged and can be reused
what are the factors affecting rate of enzyme action
temperature
pH
substrate concentration
enzyme concentration
how TEMPERATURE affects rate of enzyme action
increase in temperature → increase in kinetic energy of enzyme and substrate molecules
increase in effective collisions → more enzyme-substrate complexes formed per unit time
rate of reaction increases with temperature until optimum temperature of 30℃-40℃ (enzyme functions at max rate) is reached
increase beyond optimum temp → denatured enzyme → rate of enzyme action decreases
what happens when enzyme is denatured
enzymes are made out of proteins. excessive heat disrupts the intermolecular bonds which stabilise the structures of the enzyme
enzyme unfolds and precise shape of active site is lost
denaturation is irreversible
what happens when enzyme is placed near freezing point
inactivated
enzyme activity is very low
goes back to normal when higher temperatures are restored
how pH affects enzyme activity
enzyme at optimum pH (maximum rate of reaction occurs)
conformation of active site most ideal for substrate binding
highest frequency of effective collisions
greatest no. of enzyme-substrate complex formed per unit time
what happens to enzyme activity at pH higher or lower than optimal pH
H+ concentration changes
alters bonds that help maintain conformation of enzyme
active site and substrate binding will be affected
normally reversible
denatured at extreme pH changes
how does substrate concentration affect enzyme activity
increase in substrate molecules
increase in frequency of effective collisions
more enzyme substrate complexes formed per unit time
rate of reaction increased
why does the increase in substrate concentration produce no change at a certain point
all active sites of enzymes are currently occupied with substrate molecules
extra free substrate molecule has to wait for products to be released
how does enzyme concentration affect enzyme activity
increase in enzymes
increase in frequency of effective collisions
more enzyme substrate complexes formed per unit time
rate of reaction increased