23. Write free energy change (AG), standard free energy change (AG), and biochemical free energy change conditions (AG") (leave blank if something doesn't apply to the condition) Temperature Pressure Reactant's initial conc. [H+] conc. [H₂O] Free energy change standard free energy (AG) change (AG") Biochemical standard free energy change (AG")
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23. Write free energy change (AG), standard free energy change (AG), and biochemical free energy
change conditions (AG") (leave blank if something doesn't apply to the condition)
Temperature
Pressure
Reactant's initial conc.
[H+] conc.
[H₂O]
Free energy change standard free energy
(AG)
change (AG")
Biochemical standard
free energy change
(AGI)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F84f39a0e-1c16-43ec-bcb3-7f889ca233a2%2Ff7deb506-bb8d-445e-891c-a25515b8d3a3%2Fljrfkh_processed.jpeg&w=3840&q=75)
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- Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?Please ASA. Thanku. In the reaction Na + Cl à Na+ + Cl-, which component is said to become ‘oxidized’ and which is considered reduced? Na, Cl Cl, Cl Na, Na Cl, Na6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
- Arachidonic acid, a 20-C saturated fatty acid. Use only 1 mole:1. How many rounds of beta-oxidation are needed to oxidize the fatty acid, and what is the total ATP yield? Show your solution.Trend observed in graph and conclusion about the effect of temperature on enzyme activity. i) include a concise description of the trend observed in the graph shown in question 3 above, and explain this trend using the language presented in this unit and your biochemical knowledge of enzymes and reactions. In your conclusion, provide a logical argument supported by molecular theory that would explain any change observed in enzyme activity.Select all that apply. What are the functions of ATP?
- ch Select all statements that are correct. Note there might be more than 1 correct statement. From the Lineweaver-Burk plot the equilibrium constant (Keq) can be obtained The Lineweaver-Burk plot gives a more accurate prediction for Vmax than the Michaelis- Menten plot The Lineweaver-Burk plot assumes that products and reactants are present at equal concentrations during the entire time of the reaction The Lineweaver-Burk plot shows velocity of reaction vs substrate concentration The Lineweaver-Burk plot shows 1/velocity of reaction vs 1/substrate concentration O 20°C D) // EA particular enzyme has a ΔΔG‡ of -22.1 kJ mol-1 at 37.0 °C. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)Make a v vs. [S] plot for an enzyme that obeys Michaelis-Menten kinetics with a Vmax of 150 mM/min and Km of 1.5 mM.