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
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: 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 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
The amino acid glycine is often used as a component of buffers in biochemical experiments. The amino group of glycine has a pKa of 9.6, which can exist in the protonated form -NH3+ or the free base -NH2 as shown in this equilibrium:
R-NH3+ ⇌ R-NH2 + H+
(a) Using glycine as a buffering agent requires specific pH ranges. Identify the buffer range for glycine’s amine group and describe how this molecule provides buffer capabilities as small amounts of HCl(aq) is added to the solution.
(b) In a 0.1 M solution of glycine at pH = 9, what fraction of glycine has its amino group in the -NH3+ form?
(c) When 90% of glycine is in its -NH3+ form, what is the numerical difference between the pH of the solution and the pKa of the amino group?
In: Biology
In: Accounting
30.0 uM(microMolar) solution of enzyme catalyzed breakdown of 0.250M of substrate in 2 minutes. How many molecules of substrate were converted to product each second by one enzyme molecule?
In: Chemistry
1. Describe the link between understanding enzyme mechanism and drug design and development.
2. How does regulation of 1 enzyme in a metabolic pathway modulate the flux through the entire pathway?
In: Chemistry