What is the purpose and/or products of the following steps?
Question 1 options:
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In: Biology
_______________________ are stripped from the intermediate organic molecules of the Krebs Cycle.
carbon and hydrogen atoms
oxygen and electrons
H+ and electrons
ATP and NAD
In aerobic respiration NADH and FADH2 are oxidized back into NAD+ and FAD by
glycolysis.
the Krebs Cycle.
the electron transport chain.
fermentation.
Two ATP are used to add two phosphate groups to glucose in the
Krebs Cycle.
electron transport chain.
glycolysis.
bridge step.
ATP and ________________ is/are the product(s) from the Krebs Cycle.
NADH
FADH2 and NADH
NADH and carbon dioxide
NADH, FADH2 and carbon dioxide
NADH, FADH2, carbon dioxide and oxygen
In: Biology
1. Binding energy between an enzyme and a substrate contributes to catalysis in which way?
A. Binding energy provides the enzyme specificity for the substrate
B. binding energy contributions allow for entropy reduction in the substrate-enzyme complex
C. binding energy compensates for energy changes as a result of desolvation of the substrate
D. binding energy contributes to the process of induced fit between the substrate and the enzyme
E. all of the above are correct
2. a reaction is spontaneous if..
A. the transition state has higher free energy that the substrate
B. the product has lower free energy that the substrate
C. it proceeds rapidly and without a catalyst
D. it can proceed in only on direction
3. the enzyme Pepsin is produced in the stomach lining initially as a _______, which requires _______ for activation in the stomach.
A. Kinase; phosphorylation
B. zymogen; irreversible proteolytic cleavage
C. proprotein; reversible proteolytic cleavage
D. zymogen; ubiquitination
E. phosphorylase; irreversible proteolytic cleavage
In: Chemistry
1. If the enzyme-catalyzed reaction E + S ↔ ES ↔ E + P takes place near Vmax to the enzyme (E), what can be concluded about the relative concentrations of S and ES?
a) High [S], [ES] is low
b) High [S], [ES] are at their maximum
c) Low [S], [ES] is low
d) Low [S], [ES] is at its maximum
2. Which of the following statements about Michaelis-Menten kinetics is correct?
a) Km = the substrate concentration required for the reaction to reach Vmax
b) Km = dissociation constant of the enzyme-substrate complex
c) Km = is a measure of the substrate's affinity for the enzyme
d) Km = expression of reaction rate
3. What is the Km value if the substrate concentration is 25 mM and the initial reaction rate is half Vmax for an enzyme catalyzed reaction?
a) Km = 50 mM
b) Km = 12.5 mM
c) Km = 625 mM
d) Km = 25 mM
In: Chemistry
In: Biology
1. Describe how attaching an enzyme to the cell membrane regulates the rate of a specific reaction
2. Describe the type of reaction that is typically regulated by an allosteric enzyme based on DG for the reaction.
3. Differentiate between positive and negative feedback loops based on sequence of reactions resulting the formation of a final product, “F”
4. Differentiate between the [S] that gives half maximum velocity based on an allosteric enzyme without and with an allosteric activator
In: Biology
1. Describe the function of the following enzymes: glycogen phosphorylase, glycogen synthase, protein kinase a, adenylate kinase, branching enzyme
2. a. Why do cell extracts require NAD+ to convert glucose to pyruvate? What intermediates accumulate when NAD+ is absent? Explain. b.Why does the rate at which glucose is converted to pyruvate decrease when citrate is added?
3. Define gluconeogenesis. What molecules are good substrates for gluconeogenesis? Biosynthetic and catabolic pathways are rarely identical. Is this true for gluconeogenesis vs. glycolysis? Explain.
4. a. How does a D-glucose differ from B D-glucose? b.What is the difference between a 1-6 bond between two glucose molecules and a 1-4 bond? c.What is the difference between fructose and glucose? d.How does ribose differ from glucose? e.Carbohydrates (glucose, for example) are frequently phosphorylated upon entering a cell. Why?
5. Determine whether the following statements regarding free energy change are true or false. If false, change them to make the statement true.
Free energy change is a measure of the speed of the reaction.
Free energy change is a measure of the maximum amount of work available from the reaction.
Free energy change is a constant for a reaction under any conditions.
Free energy change is equal to zero at equilibrium.
The hydrolysis of ATP proceeds with a negative G.
In: Chemistry
The choice of acid is important in the dehydration reaction. The following acids are not suitable for dehydration of 2-butanol: acetic acid and hydrobromic. Explain why each of the acids would not be a good choice to affect the dehydration in good yield.
In: Chemistry
In: Accounting
The amino acid glutamic acid has the molecular formula C5H9NO4, and the amino acid isoleucine has the molecular formula C6H13NO2. Determine how many moles of isoleucine contain the same number of atoms as 1.96 mol of glutamic acid.
In: Chemistry