1.provide a solution using a table, listing all the specific individual reactions that willgenerate ATP either by substrate level phosphorylation (SLP) or by oxidativephosphorylation (OP). 2. Shall the given question require a shuttle system, please use bothand indicate the net ATP for each. 3. Get the net ATP for each question given youSpecific reactionNumber of ATP (+ or -)Question 1: fructose 6-phosphate to 2acetyl coaQuestion 2: fructose 6-phosphate to 6C02Question 3: fructose 6-phosphate to 2succinyl coa

Metabolism includes biosynthesis/ reduction (an anabolic process) and oxidation (catabolic…

Answered: 1.provide a solution using a table,…

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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7) The following questions apply to glycolysis (figure 3-41 on page 79 of the 12th edition), the Krebs cycle (figure 3-44 on page 82) and to oxidative phosphorylation (figure 3-45 on page 84). Calculate the total amount of ATP produced from one glucose molecule if: a. The oxidation of NADH + H* to NAD* + 2H* produced 4 ATP. b. The oxidation of FADH₂ to FAD + 2H* produced 1 ATP. c. Each step of the Krebs cycle that produces NADH+H* produced FADH2 instead. d. Each step of the Krebs cycle that produces FADH2 produced NADH + H+ instead. e. Sucrose is substituted for glucose.
Please answer fast The equilbrium constant (Keq) under standard conditions for the hydrolysis of ATP is 200,000 M. This would suggest the reaction is: 1. proceeding in reverse direction 2. proceeding in forward direction 3. in equilibrium However, this does not take into consideration the concentration of substrates/products within the cell. This is can be calculated by determining the reaction quotient, Q by: [ATP] x [Pi] / [ADP] [ATP] + [Pi] / [ADP] [ADP] x [ATP] / [Pi] [ADP] x [Pi] / [ATP] Biochemical reactions commonly involve the transfer of groups from ATP. What is one of the products of pyrophosphate cleavage from ATP? AMP Adenosine ADP Inorganic phosphate Q5-6. The hydrolysis of ATP is often coupled to other reactions. For example: Phosphoenolpyruvate (PEP) + H2O → Pyruvate + Pi (ΔG'° = -63.1 kJ/mol) ATP + H2O → ADP + Pi (ΔG'° = -30.5 kJ/mol) (The standard free-energy changes for the reactions are indicated in brackets) Q5. Given the information above, what is the…
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
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PLEASE ONLY ANSWER PART D OF THIS QUESTION.
3. The reaction shown below is catalyzed along the pathway of glycolysis by an enzyme with the active site architecture shown. A. The enzyme has two Mg2+ ions, a lysine general base (deprotonated) and a glutamate general acid. In the box below, draw a plausible mechanism for this reaction, which has two formal steps with one intermediate between them (hint: one step uses the general acid and the other uses the general base.) O +(87 -00 11 R-00 00 00 + H₂O OH O Mg2+ Mg2+ Lys (general base) NH₂ OH Glu (general acid) enzyme active site
You are isolating mitochondria from insect cells and incubating in a test tube with 0.005 M FADH2, 0.05 M ADP and 0.05 M Pi. Assuming, these 3 can enter mitochondria at no cost,no glucose/products of glucose metabolism remain in the isolated mitochondria, and oxygen is present. Part 1) If all expected reactions go to completion, how much ATP is expected formed? (0 M)(0.02 M) (0.03 M) (0.05 M) (0.1 M) (0.005 M) (0.01 M) (0.015 M) Part 2) The ratio of FADH2/FAD at completion of all expected reactions would be? (2) (>>2) (0) (1) Part 3) After completion of all expected reactions, ratio of H ion concentration inside vs. outside the mitochondrial inner membrane should be? (<1) (~1) (>1)(0) Please provide brief explanation
Write the No of ATP yield for EMP cycle. To do accounting, write the reaction and show the ATP formed. Assume that for 1 mole of glucose, two EMP cycle is executed.
2.3
1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain
These are the results from my experiment of determining the optimal temperature for amylase. The question I have is what is the optimal temperature of the reaction? (Would it be 55 degrees Celsius?) and at what temperature does amylase denature...my guess is 65 degrees

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