Consider the following reaction occurring at 298 K:OHCH₂OHOH-0. OHOH+ATPk₁k₂0-OCH,OHOH0 OHOHGlucoseGlucose 6-phosphateHexokinase is an enzyme that catalyzes this reaction. When the hexokinase ispresent the rate of k₁ is 1.3 X10-3 M-15-1Calculate the activation energy for the hexokinase catalyzed forward reaction..+ADP

Biochemical reactions tend to be slow because biomolecules are stable at biological pH and…

Answered: Consider the following reaction…

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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Similar questions

Write a balanced equation for the overall reaction occurring in this system, showing oxidation of the initial electron donor, reduction of the final acceptor, and synthesis of ATP.
Allosteric regulation plays a very important role in the regulation of glycogen metabolism. Which of thefollowing is correct? -AMP allosterically inhibits glycogen phosphorylase -Glucose-6-phosphate allosterically activates glycogen synthase -Both A and B -Neither A nor B The value of standard free energy change for reaction A --> B is +3.7 kJ/mol. Under which of thefollowing conditions, the reaction will most likely become exergonic in the direction as written? -Mass action ratio is larger than the equilibrium constant -Couple with ATP hydrolysis -Both A and B -Neither A nor B
Could you help propose a reasonable mechanism for the following biochemical transformation?
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
Match group A and group B
One process catalyzed by NADHNADH dehydrogenase is NADH+H^++ubiquinone ↽−−⇀ NAD+ubiquinolNADH+H^++ubiquinone ↽−−⇀⁢ NAD^++ubiquinol The standard reduction potentials for the half‑reactions are given in the table. Oxidant Reductant ?′0 ubiquinone+2H++2e−ubiquinone+2⁢H++2⁢e^− ubiquinolubiquinol 0.045 NAD^++H^++2e−NAD^++H^++2⁢e^− NADHNADH –0.32 Calculate Δ?′0 for the reaction as shown. Δ?′0=____(V) Calculate Δ?′0 . Δ?′0=____(kJ/mol)
In glycolysis, fructose 1,6-bisphosphate is converted to two products with a standard free- energy change (AG) of 23.8 kJ/mol. Under what cellular conditions will the free-energy change be negative, enabling the reaction to proceed spontaneously to form products? O In a cell where the concentrations of products and reactants yield a low value of the mass-action ratio Q ○ The reaction will not go to the right spontaneously under any conditions because the AG is positive ○ The reaction will proceed spontaneously to the right if there is a high concentration of products relative to the concentration of fructose 1,6-bisphosphate ○ The reaction will proceed spontaneously to the right if there is a high concentration of enzyme to catalyze the reaction O None of these conditions is sufficient
Find the net ΔG° of the reaction.
This is a picture of the catalysis of alcohol by ADH with an inhibitor binding as an aldehyde analog. I have two questions. First, what would the enzyme be classified as and why? Also, what would the steps of this mechanism be?
can you explain what is happening in the attached graph? Figure 3: Lineweaver-Burke plot of alkaline phosphatase activity without inhibitor
Provide a reasonable step-wise mechanism for the reaction below, involving TPP as acoenzyme (can abbreviate the pyrophosphate as R), and invoking any general acids or base fromacetolactate synthase that you might need .
Why does ATP hydrolysis release so much energy? O Hydrolysis increases entropy through a gain in the possible resonance structures for Pi versus a terminal phosphate O Hydrolysis decreases entropy through a loss in the possible resonance structures for Pi versus a terminal phosphate O Hydrolysis decreases enthalpy through a loss in the possible resonance structures for Pi versus a terminal phosphate O Hydrolysis increases enthalpy through a gain in the possible resonance structures for Pi versus a terminal phosphate

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