BCH 361 Ch. 6 Study Questions with 100% Correct Verified Solutions| Latest Update
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Course
BCH 361
Institution
BCH 361
Which describes how cofactors and coenzymes affect the function of enzymes?
A. increase or decrease catalytic function
B. increase catalytic function
C. do not impact catalytic function
D. decrease catalytic function - Answer B
BCH 361 Ch. 6 Study Questions with 100%
Correct Verified Solutions| Latest Update
Which describes how cofactors and coenzymes affect the function of enzymes?
A. increase or decrease catalytic function
B. increase catalytic function
C. do not impact catalytic function
D. decrease catalytic function - Answer B
The lock and key model and the induced fit model are 2 models of enzyme action
explaining both the specificity and the catalytic activity of enzymes. Indicate whether
each statement is part of the lock and key model, the induced fit model, or is common
to both models.
A. the substrate binds to the enzyme at the active site, forming an enzyme-substrate
complex
B. the enzyme active site has a rigid structure complementary to that of the substrate
C. the substrate binds to the enzyme at the active site, forming an enzyme-substrate
complex
D. the enzyme conformation changes when it binds the substrate so that the active site
fits the substrate - Answer lock and key model: B
induced fit model: D,
common to both models: A, C
When considering free energy change, biochemists usually define a standard state, the
biochemical standard state, which is modified from the chemical standard state to fit
biochemical applications.
Determine which of the phrases describe the biochemical standard state, the chemical
standard state, or both
,A. ∆G°
B. the pressure is 1 atm
C. the temperature is 25 degrees Celcius
D. [H+]= 10^-7 M
E. constant value for [Mg2+]
F. the initial concentration of the reactants and products is 1 M
G. pH 0
H. ∆G°' or ∆G'°
I. the change in [H20] is assumed to be insignificant - Answer Biochemical standard
state: D, E, H, I
Chemical standard state: A, G
Both: B, C, F
Why are proteins well suited to be catalysts? - Answer their capacity to form complex
3D structures that can recognize one or a few molecules (their substrates) w/ high
specificity at a particular site on enzyme called active site, where the substrates are
oriented and brought into close proximity to facilitate the chemical reactions
Enzymes are characterized by: - Answer catalytic power, specificity to substrate,
specificity to a type of rxn
allosteric enzymes have active sites that can be modified by what - Answer cellular
environmental signals like endogenous small molecules
enzymes - Answer are proteins catalysts that can accelerate the rate of a rxn
, carbonic anhydrase - Answer fastest enzyme known; facilitate transfer of CO2 from
tissue to blood and from blood to lung (accelerate both forward and backward
directions)
Nonenzymatic half- life of OMP decarboxylase - Answer 78,000,000 years
Nonenzymatic half-life of AMP nucleosidase - Answer 69,000 years
Nonenzymatic half-life of Triose phosphate isomerase - Answer 1.9 days
Nonenzymatic half life of Carbonic anhydrase - Answer 5 seconds
Uncatalyzed rate of OMP decarboxylase - Answer 2.8 * 10^-16
Uncatalyzed rate of AMP nucleosidase - Answer 1.0 * 10^-11
Uncatalyzed rate of Carbonic anhydrase - Answer 1.3 * 10^-1
Catalyzed rate of OMP decarboxylase - Answer 39
Catalyzed rate of AMP nucleosidase - Answer 60
Catalyzed rate of Triose phosphate isomerase - Answer 4,300
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