Lesson 15 - Product time graphs continued & factors affecting enzyme controlled reactions Flashcards
For an enzyme to catalyse a reaction, it must…
- Come into physical contact with a substrate(s)
- The substrate must be complementary to the active site
= SUCCESSFUL COLLISION!
What is activation energy?
The minimum energy required for molecules to react (breaking existing bonds/making new ones)
What determines the shape of an enzyme’s active site?
Tertiary structure – held in place by selection of bonds – ionic/disulphide/hydrogen (which is in turn determined by amino acid sequence (primary structure))
Name 4 factors that could affect the rate of enzyme action?
Temperature
pH
Enzyme concentration
Substrate concentration
Formula for rate of reaction
change in product/change in time
Enzyme concentration against rate of reaction graphs:
- begins with 0 rate of reaction
- as enzyme concentration increases, RoR increases
- after a point, the graph plateaus, meaning the RoR stays constant and substrate concentration is the limiting factor
Substrate concentration against rate of reaction graphs:
- begins with 0 rate of reaction
- as substrate concentration increases, RoR increases
- after a point, the graph plateaus, meaning the RoR stays constant and enzyme concentration is the limiting factor
Define a limiting factor
A factor is limiting when an increase in its value causes an increase in the rate of reaction
what is V-max
the maximum velocity (ie rate) at which the enzyme catalysed the reaction – happens when all enzyme active sites are saturated with substrate
What is pH?
A measure of its hydrogen ion concentration (H+)
The pH of a solution is calculated using the formula:
e.g. a hydrogen ion concentration [H+] of 1 x 10-9 therefore has a pH of 9
Why do scientists measure the initial rate of reaction of enzyme-catalysed reactions?
they measure the rate at the start of a reaction before any factors, e.g. substrate concentration, have had time to change.
Temperature against rate of reaction graphs:
- increase in KE, molecules move faster, more successful collisions, more E-S complexes and faster RoR
- the peak of the curve, optimum temperature. (Highest KE before denaturation)
- enzyme denatures, change in shape of enzyme’s active site. It’s no longer complementary to substrate, can’t bind, no E-S complexes, decrease in RoR
pH against rate of reaction graphs:
- a peak on the graph: optimum pH
- on either side of the peak, the enzyme denatures. Which means its no longer complementary to substrate, can’t bind, no E-S complexes formed, so a decrease in rate of reaction