factors affecting enzyme activity Flashcards
how can you measure enzyme activity
how fast the product is being made
how fast the substrate is being broken down
what are the factors affecting enzyme activity
temperature
pH
substrate concentration
enzyme concentration
how does temperature increase rate of enzymes
the enzyme controlled reaction increases when the temperature increases, more heat means more kinetic energy so molecules move faster, this makes substrate molecules more likely to collide with the enzymes active site
what happens if the temperature gets too high
the reaction will stop, it causes the enzymes to vibrate if the temperature gets too high these vibrations will break some of the bonds that holds the enzymes shape, the active site changes shape and the substrate no longer fits to the active site of the enzyme. This means it has denatured
how does pH increase enzymes rate of reaction
all enzymes have an optimum pH value, at the optimum pH enzyme activity increase, if the pH is too high the enzyme will denature.
how can substrate concentration increase enzyme activity
the higher the substrate concentration, the faster the reaction, more substrate molecules means more collisions between the enzyme and the substrate so therefore more active sites will be occupied. after that all active sites are full so no further effect takes place
what happens to the graph when the substrate concentration is high and all the enzymes have been filled
the graph will plateau
how does enzyme concentration affect enzyme activity
the more enzyme molecules there are, the more likely an enzyme will collide with a substrate and form an enzyme-substrate complex. however when the substrate amount is limited, an increase in enzyme concentration will have no effect
what are the two enzyme inhibitors
competitive and non-competitive
explain how a competitive inhibitor prevents enzyme activity
they have a similar shape to a substrate, then then compete with the substrates to bind with the enzymes active sites so no more reactions take place. They block the active site so no more substrate molecules can fit in
explain how a non-competitive inhibitor prevents enzyme activity
they bind to the enzyme away from its active site, this causes the active site to change shape so the substrate molecule can no longer bind to it
if you increase the substrate concentration while non competitive inhibitors are present what will the happen
nothing, this is because the non competitive inhibitors do not compete with the substrates as they don’t bind to the active sites
