Chapter 62
1.
a. The active site of an enzyme is the specific part that the substrate binds to. This
relates to tertiary structure as the active site is formed by the protein’s tertiary
structure which creates a precise configuration in which the amino acid side chains
can interact with the substrate
b. The active is specific because of how the protein folds up
2. Substrate molecules come into contact with an enzymes active site through collision
3.
a. Macromolecules are too big to enter the cell directly and must be broken down to
smaller molecules
b. Extracellular enzymes, such as trypsin, could damage internal proteins if produced in
an active form
Chapter 63
1. The lock and key model involves a perfectly fitting substrate being pulled into the active site.
The deficiencies of this model include that if the substrate does not fit, the reaction did not
occur, indicating that the substrate must show complete specificity.
2. The induced fit model is different because the substrate binds to the active site and changes
shape to fit and improve binding. The induced fit model has broad specificity unlike the lock
and key model
Chapter 66
1. Competitive inhibition is when the inhibitor competes with the substrate for the active site
and once in place prevents substrate binding. Non-competitive inhibition is when the
inhibitor binds with the enzyme at another site that is not the active site, making it less likely
to perform its catalytic function
2.
a. In competitive inhibition, increasing the substrate concentration can cause the rate
of reaction to return to normal, as if there was no inhibitor. The rate of reaction will
slow but eventually reach the same level achieved without an inhibitor. However in
non-competitive inhibition the rate of reaction will be slowed and can not return.
Rate depression can not be overcome by increasing the substrate concentration
b. If increasing the substrate concentration overcomes the rate depression, then the
inhibition is competitive. If not it is non-competitive.
Chapter 65
1. (2.4 – 1.4) divided by (129 – 69) = 0.017 cm^3s^-1
2.
a. (3.4 – 2.4) divided by (122 – 54) = 0.015 cm^3s^-1
b. (2.5 – 1) divided by (50 – 10) = 0.0375cm^3s^-1
3.
a. Reactants must being constantly added to the mix to ensure the graph does not
plateau.
b. After a certain point the activity plateaus as there is not enough substance to bind
and form complexes. The reactants are being used up
4. .
a. The rate of reaction will continue to increase as the concentration will continue to
increase
b. To vary the amount of enzymes present a cell can increase the rate of protein
synthesis
5. The reaction rate will increase until the enzyme is saturated then it will remain static
6. .
a. Optimum temperature is the temperature where the enzyme activity is at the
highest level
b. Enzymes perform poorly at low temperatures because the rate of reaction decreases
in low temperatures
c. Q10 = 1.88
7. .
a. Pepsin = 1, Trypsin = 8, Urease = 7
b. Pepsin suits acidic environments as the stomach is acidic. Trypsin works in alkaline
environments because the small intestine is alkaline. Urease works best in neutral
environments because it is found in soil, a neutral environment.
Chapter 70
1. Activation Energy (A), Active site (C), anabolic reaction (D), catabolic reactions (G), catalyst
(B), denaturation (H), enzymes (E), induced fit model (F)
2. .
a. The substrate is sucrose
b. Glucose and fructose
c. Sucrase
3. Irreversible competitive inhibitors permanently stop enzyme activity, thus the enzyme is non-
functional. This can shut down important metabolic pathways (cellular respiration)
4. .
a.
5. .
a. Competitive
b. A
6. Increasing surface area for reactions and compartmentalisation
7.
