Question 2 of 13Fill in the blanks:WriteC if only statement A is correct,H if only statement B is correct,E if both statements are correct,M if both statements are incorrect.A. The Michaelis-Menten plot shows that initially, the increase in the reaction velocity isrelatively fast.B. Then after sometime, the change in the reaction velocity slows down and tapers off to a certain limit.

Michaelis-Menten plot shows thta initially the increase in the reaction velocity is relatively fast…

Answered: Question 2 of 13 Fill in the blanks:…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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QUESTION 1 a. John has just taken his Lunch meal, after which he is going to takes his Daily soccer practice match in the next 30 min, how will glycolysis operate/work in such conditions or be applicable b. How will oxidative phosphorylation work in sickly John who usually practice daily in soccer? Make possible scenarios c. Enzymes are critical in the metabolism of most most organic compounds, actually 30% of reactions are catalysed by them. How would the inactive enzymes (Sickness) in electron Transport Chain compromise the fat breakdown in the body.
Question 1: Part a: Assume that the standard free energy of ATP hydrolysis is -31 kJ/mol. Assume the following values for the standard free energy changes of the four reactions: HK -16.7 kJ/mol; PFK -14.2 kJ/mol; PGK -18.9 kJ/mol; PK -31.7 kJ/mol. (from bio.libretexts.org). Use these values to compute the standard free energy of hydrolysis (releasing Pi) of i. glucose 6-P ii. fructose 1,6-bis-P iii. 1,3-bisphosphoglycerate iv. phosphoenolpyruvate Part b: Which of these four compounds is the strongest phosphoryl donor?______________ Which is the weakest?__________________ Part c: The phosphoglycerate kinase reaction is favorable by -18.9 kJ/mol in the glycolytic direction, as stated above. In gluconeogenesis, this step is simply reversed; i.e. it is not one of the three steps in gluconeogenesis that is driven by using different chemistry than that of glycolysis. How can this be? (Be specific: what specific factors could enable reversal of this step?)
QUESTION 6 Which of the following statements are true about enzyme inhibitors? QUESTION 6 Which of the following statements are true about enzyme inhibitors? A. Competitive inhibitors cause the slope of the Lineweaver-Burk line to change but not the y-intercept. B. Noncompetitive inhibitors are a type of mixed inhibitors. C. Uncompetitive inhibitors result in an alpha equal to 1 and an alpha' not equal to 1. D. Noncompetitive inhibitors result in lines with increasing [I] to share the same x-intercept. all of the above E. All of the above are true.
SITUATION:You are a chemist in a manufacturing company which produces acetaldehyde, CH3CHO. This is prepared by the reaction of ethanol with copper (II) oxide according to the following equation: CH3CH2OH + CuO → CH3CHO + H2O + CuIf there are 1620 g of ethanol and 1020 g of CuO readily available in the laboratory, what mass of acetaldehyde can be produced? QUESTIONS: 1. Would you recommend the company to buy more ethanol or copper (II) oxide? Why?2. How many grams of acetaldehyde will be produced from the readily available materials?3. How many grams of the excess reactant will be left after the reaction?4. If your actual yield is 552.6 g, what is its percent yield?
A. Will decreasing the amount of energy needed to make an exergonic reaction occur cause the reaction to be more exergonic? Why or why not? B. Will such an energetic alteration change the rate of the reaction? Why or why not
Question 19 Which of the following would have the lowest (most negative) standard reduction potential (E’0)? a FADH2 b Glucose c O2 d NADH
The following exothermic reaction is at 0.00 °C and 1.00 atm SeO4 (g) ⇌ Se(g) + O2(g) , kc = 2.4 ×10-6 The reaction contains [SeO4] = 0.100 M, [Se] = 0.0034 M, [O2] = 0.0022 M Does the reaction exist at equilibrium? If not, in what direction it will proceed? Question 22 options:
Regarding the reasoning for the Michaelis-Menten equation to be unsuitable for accurate analysis of experimental data, select all that apply: It is nonlinear It is only valid for reactions at equilibrium It is not valid under experimental conditions Extrapolation to Vm is inaccurate and therefore Km also cannot be accurately described
Can the thermodynamic property Δ G° be used to predict the speed of a reaction in a living organism? Why or why not?
The first and second laws of thermodynamics are useful for biochemists who investigate chemical reactions in living organisms. Explain why the third law is not useful.
The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor will have the same 1. Vmax2. Km3. Km/Vmax4. 1/Vmax
Skeletal muscle can store energy in the form of phosphocreatine, which is able to regenerate ATP. In relation to this, answer all of the following: (Show all your work for each part) a) Use your knowledge of bioenergentics to show why this statement is true. b) What is K¢eq for the overall reaction? c) Drawbiochemicalstructuresfortheoverallreaction. d) If the steady-state concentrations of phosphocreatine and creatine in a myocyte (muscle cell) are 1 uM and 129 uM, respectively, what will be the ratio of [ATP]/[ADP], assuming the creatine kinase reaction is at equilibrium?

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