**Question 6**First reaction: \( X + Pi \rightarrow X\text{-}phosphate + H_2O \), \( K_{eq1} = 15 \)Second reaction: \( ATP + H_2O \rightarrow ADP + Pi \), \( K_{eq2} = 10 \)For the coupled reaction: \( ATP + X \rightarrow ADP + X\text{-}phosphate \)What is \( K_{eq} \) for the coupled reaction?a. 50 b. 2 c. 150 d. 15

Adenosine triphosphate (ATP) hydrolysis : the catabolic reaction process in which release of…

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Biochemistry

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ISBN:9781319114671

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

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Chapter1: Biochemistry: An Evolving Science

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P2.5
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. Write a balanced equation for the complete oxidation of each of the following, and calculate the respiratory quotient for each substance. (a) Ethanol (b) Acetic acid (c) Stearic acid (d) Oleic acid (e) Linoleic acid
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a) What is cross linking? Write down its advantages and disadvantages.
Consider the reaction catalyzed by PFK. In the presence of AMP, which of the following will be expected? Check all that apply: a)The Km for substrate would be decreased b) the initial velocity plot would show the curve shifted to the right c) the R state is stabilized d)the rate of the reaction is diminished
which yields more free energy when completely oxidized, stearate or alpha-linolenate?
. Consider the enzymatic reaction scheme: Asparagine + H20 Aspartate + NH3: a) calculate the specific activity of the enzyme, if in 30 seconds as a result of a reaction involving 3 mg of the enzyme under optimal conditions (pH 8.0, 37 °C) 75 umol aspartate is obtained; b) describe the reasons for the decrease in enzyme activity after incubation for 6. 10 minutes at 70 °C (provide an appropriate graph).
5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
Glucose CO,+X (a) State the name of the process represented by this equation, (b) Name compound X. (c) Explain why energy produced in the above process is stored in form of ATP. uocle cells
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ADP What is Keg for the coupled reaction?