The ATP hydrolysis reaction (shown below) has a AG of -31 kJ mol-1.NH2NH2Do you predict that AS is positive ornegative for this reaction. Explain in one sentence.а..NH20-OCH2OCH2EnergyPhosphate ionÓH ÓHAdenosine triphosphate (ATP)Adenosine diphosphate (ADP)b.How does the hydrophobic effect contribute to the AS you predicted in part a. Makesure to discuss the ordering of water molecules in your answer. Include a minimum of 3sentances in your explaination.

Given; ATP hydrolysis reaction depicted shows: On addition of H2O to ATP molecule energy is…

Answered: The ATP hydrolysis reaction (shown…

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 23 An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation... SHOW MORE V The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d. The V for X will be affected if Y is present in the reaction mixture. max pH dependence of Vmax reflects the ionization state of catalytic site e residues. Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X = 0.01 M and the Km for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of g products to reactants (Keg).
I need help with parts d-g a.) For Ado: catalytic efficiency = 4.18 x 106 M-1s-1 For ATP: catalytic efficiency = 12.1 x 107 M-1s-1 b.) Both specificity constants are below the diffusion limit so neither substrate is limiting the reaction rate due to diffusion c.) Line weaver Burk equation for AdoK enzyme with Ado substrate: y = 0.68x + (2.04 x 104), where y = 1/vo and x = 1/[Ado]
Given the following choices,a. what is the structure of the product of the reaction catalysed by ACAT?b. structure of the product produced from the reaction catalysed by phospolipase A2?c. general structure of TAGd. structure of glycerol
The following is the chemical structure of nicotinamide adenine dinucleotides, a coenzyme commonly used in enzymatic reactions. Но 4 HO 0-P-0 *Na "O. `NH2 N 1 "OH H2N OH Which of the indicate regions is the site of the redox activity of this coenzyme? 2.
Can you explain the answe?
In the given reaction below, the amino acid NH₂ KMTs undergoes CH3 H3C-N* CH3 reaction.
In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?
The free energy change of each step of glycolysis is given in the table below. ∆G°’ is the free energy under standard conditions (25°C, 1M each reactant, pH 7), while ∆G is the free energy change at presumed physiological conditions. Why must no step have a positive ∆G under physiological conditions?
Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH2OH CH2OH CH2OH CH2OH он он OH OH + H20 OH OH OH но H. но но OH OH OH OH OH OH A. Oxidoreducatase B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO "ooc-CH2-CH2-C-COO Amino acid a-Ketoglutarate
The table contains data about how different ASFV mutants affect enzyme activity-- for example the D29A mutant, where the D at position 29 was mutated to an A. Select three mutants at random, and for each mutant explain how that mutation could affect intermolecular force interactions (an example: hydrogen bonding could be disrupted by this mutation because…
Select the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the above
In order to function as an oxidative phosphorylation uncoupler (page 648), 2,4-dinitrophenol must act catalytically, not stoichio- metrically. What does this mean? Identify and discuss an important implication of this conclusion.

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