Consider the reaction catalyzed by PFK. In the presence of ATP, which of thefollowing will be expected? Select all that apply.The T-state is stabilizedThe rate of the reaction is enhanced.The initial velocity plot would show a shift in the curve to the rightThe quaternary structure of PFK is stabilized to promote efficient binding of substrate

Phosphofructokinase-1 (PFK-1) is a glycolytic enzyme that catalyzes the transfer of a phosphoryl…

Answered: Consider the reaction catalyzed by PFK.…

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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Give all the reactions that will produce ATP either by substrate-level phosphorylation (SLP) or by oxidative phosphorylation (OP). If the given require a shuttle system, please indicate both MA shuttle and GP shuttle and give the ATP produced. Given: fructose 6-phosphate to 2pyruvate
Many metabolites are maintained at steady‑state concentrations that are far from equilibrium. A comparison of ?′eq and ? , the mass‑action ratio, can determine whether a metabolic reaction is far from equilibrium. The equation for this equilibrium is, fructose 6-phosphate+ATP↽−−⇀fructose 1,6-bisphosphate+ADPCalculate ?′eq for this reaction at ?=25.0 ∘C . Δ?∘′=−14.2 kJ/mol ?′eq=
In vivo, ATP is usually bound to magnesium or manganese ions. Why is this the case?
V-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits and ATPIADP + Pj of the F-class synthase. Which of the following associations between the conformation of the beta subunit and ATP/ADP + P¡ is correct for V- Binding Change Mechanism loose binding ADP+P ATP ATP class pumps? C repeat ADP + P, ADP АТР tight binding АТР +P оpen АТР O The open conformation releases ATP. Hydrolysis of ATP to ADP + P¡ drives the change from tight to loose. O Binding of ADP + P¡ drives change from open to loose. Hydrolysis of ATP to ADP + Pj drives the change from open to loose.
Can you explain the answe?
a Construct a graph showing the initial rates of reaction of the enzyme catalase over the substrate concentration range of 4–14 vol hydrogen peroxide in the presence and absence of heavy metal ions. b Explain to what extent this data supports the hypothesis that copper ions are a non-competitive inhibitor of the enzyme that decomposes hydrogen peroxide.
The above reaction coordinate diagram in the presence of enzyme is inconsistent with the "lock and key" model of enzyme-substrate l binding. Draw and properly label the reaction. coordinate diagram for the enzymatic reaction according to the "lock and key" model. Explain why this model is inconsistent with catalytic properties of enzymes.
Consider the following mechanism: What kind of reaction is occurring during this step of glycolysis? What metabolite is in Box 1? What metabolite is in Box 2? What metabolite is in Box 3? What enzyme catalyzes this reaction? Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*
assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?
How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high substrate?
The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the micro environment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.
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

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