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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1. Provide the best coenzyme(s) for each step shown below. Give a 1–2 sentence rationale for your choice. 2. Reaction (C) can require multiple coenzymes, or the enzyme may only require one. Briefly describe how the reaction that uses only one coenzyme works. Be specific about the mechanism.
6. Examine the plot of the enzyme-catalyzed reaction below: Wheat-germ acid phosphatase shows Michaelis-Menten kinetics when acting on para-nitrophenol phosphate 16 14 12 10 8 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 (S] / mM a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What is the approximate value of Vmax? Km? c) Assuming that this plot was made at 100 nM enzyme, draw the curve, including axis labels, for 300 nM enzyme. d) Imagine that this enzyme is inhibited by a competitive inhibitor with Ki (for inhibitor) = Km (for substrate). Note that v = (kcat [E] tot [S]/Km) / (1 + [S]/Km + [I]/Ki). Draw the curve of reaction velocity (v) versus [S] for [I] = 1 mM. e) Now consider an experiment where you simultaneously introduce substrate and competitive inhibitor at equal concentrations. Make a plot of v versus concentration of [S] = [I], i.e. the X-axis should be the concentration of both I and S, which are equal. v/ uM min-
= Cellular Respiration Glucose (Cs) 2 G3P (Cs) 2 U Cs) 2 GTP- GDP (Cs) 2 acetyl CoA (___Cs) 1½/202 iii H₂O iv 2 Fill out the diagram as indicated by instructions below. Label processes g. A, B, and C. h. Some reactions are labeled with numbers in blue ovals. (Some of these are "collected" reactions, i.e. they stand for all reactions of the same type that occur in the same part of the pathway.) Among these reactions, write in reactants and products for all reactions that involve ATP and ADP. i. Reactions 6 and 8 involve FADH₂. Write in reactants and products for these reactions. j. Among the reactions labeled with numbers in blue ovals, write in reactants and products for all reactions that involve NAD+ and NADH. k. Below, write in the molecules that correspond to each of the following labels (iv is a molecule moving through the protein, indicated with an arrow): i: ii: iii: iv: 1. The blank in front of molecule (i) that you identified above is to indicate how many copies of this…
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
Consider the following types of cell and their respective conditions: i. a liver cell with non-functional malate-aspartate shuttle* ii. a skeletal muscle cell lacking oxygen iii. a cell with ATP synthase deficiency* iv. a yeast cell undergoing fermentation but with defective alcohol dehydrogenase (hint: In yeast, alcohol dehydrogenase is responsible for shuttling reducing equivalents of cytosolic NADH to the mitochondria.)* V. a brain cell with non-functional Complex II of the electron transport chain* * Assume that the deficiency is isolated and will not influence the function of other respiration components
Is this correct?
Discuss how Paul Boyer’s 18O exchange experiment helped to elucidate the formation of ATP by ATP Synthase. Discuss the experimental details. Chemical equations are essential. Discuss the results of his experiments. What did he expect to see? What was surprising about these results? What conclusions did he draw about the synthesis of ATP by ATP synthase?
Briefly Explain the mechanistic details behind how ATP is synthase makes ATP, making sure to cover why making ATP this way is referred to as "Oxidative phosphorylation"
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…
Please answer correctly
Can you show the math of the ATP gain in the steps?Like for a single pyruvate wouldn't it only be ~12.5 ATP worth
Directions: Calculate the net ATP yield when the following lipids undergo complete B oxidation. Show your solution. 1. stearic acid

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