Topic 2/7/8 - Part 1 - Pictures/Diagrams Flashcards
Draw D-ribose
Refer to picture
Draw Alpha-D-glucose
Refer to picture
Draw Beta-D-glucose
Refer to picture
Draw a saturated fatty acid
Refer to picture
Draw an amino acid
Refer to picture
Identify the biochemical
Carbohydrate (starch)
Identify the biochemical
Lipid (triglyceride)
Identify the biochemical
Lipid (steroid)
**Make sure that you know this is a lipid
Identify the biochemical
Lipid (phospholipid)
**Make sure that you know this is a lipid
Identify the biochemical
Protein
The following diagram shows an exergonic reaction without an enzyme. Draw a corresponding diagram of the reaction when it is catalyzed by an enzyme.
Refer to picture
With the help of a graph, explain how temperature affects enzyme activity
- Low temperatures result in insufficient thermal energy for the activation of an enzyme-catalysed reaction to proceed
- Increasing the temperature will increase the speed and motion of both enzyme and substrate, resulting in higher enzyme activity
- This is because a higher kinetic energy will result in more frequent collisions between the enzymes and substrates
- At an optimal temperature (may vary for different enzymes), the rate of enzyme activity will be at its peak
- Higher temperatures will cause enzyme stability to decrease, as the thermal energy disrupts the enzyme’s hydrogen bonds
- This causes the enzyme (particularly the active site) to lose its shape, resulting in the loss of activity (denaturation)
With the help of a graph, explain how pH affects enzyme activity
- Changing the pH will alter the charge of the enzyme, which in turn will alter protein solubility and overall shape
- Changing the shape or charge of the active site will diminish its ability to bind the substrate, abrogating enzyme function
- Enzymes have an optimal pH (may differ between enzymes) and moving outside this range diminishes enzyme activity
With the help of a graph, explain how substrate concentration affects enzyme activity
- Increasing substrate concentration will increase the activity of a corresponding enzyme
- More substrates mean there is an increased chance of enzyme and substrate colliding and reacting within a given period
- After a certain point, the rate of activity will cease to rise regardless of any further increases in substrate levels
- This is because the environment is saturated with substrate and all enzymes are bound and reacting (Vmax)
Draw a diagram to demonstrate competitive inhibition
Refer to picture