Which one of the following statements about the control of enzyme activity by phosphorylation is correct?a) Phosphorylationof an enzyme results in a conformational changeb) Phosphorylationof an enzyme occurs only at specific tyrosine residuesc) Phosphorylationof an enzyme is carried out by phosphoprotein phosphatasesd) Enzyme control by phosphorylation is irreversible

Kinases are enzyme that catalyzes phosphorylation reactions, which involves the transfer of…

Answered: Which one of the following statements…

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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At the left is an energy diagram that shows the energy changes for the example of glucose (C6H1206) being converted to CO2 + H2O. One curve is the reaction with enzymes, while the other is without enzymes. For these reactions, the "X" indicates: Glucose + 60g a) b) free energy of glucose free energy of activation without enzymes free energy of CO2 + H2O free energy released free energy of activation with d) e) Progrem af reaction enzymes Frec energy, G
The enzyme which catalyzes the reaction below belongs to which enzyme classification? Н.С— ОН HC=0 C=0 Н-С—ОН H,C-0-P-o- || H,C –0-P-0- O Transfera Hydrolase Isomerase Oxidoreductase
Some enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains. Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How? Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteins
Two reactions are shown below. These reactions are directly coupled in cells by an enzyme called hexokinase, which is a key enzyme in glycolysis. It is generally the case that reactions that are directly coupled by enzymes share some common reactants. What is the net reaction when these two reactions are combined? Glucose + Inorganic Phosphate + ATP + Water → Glucose 6-phosphate + ADP Glucose + ATP + Water → Glucose 6-phosphate + ADP + Inorganic Phosphate Glucose + ATP → Glucose 6-phosphate + Inorganic Phosphate Glucose + ATP → Glucose 6-phosphate + ADP
The following reaction would most likely be catalyzed by an enzyme of which class? sucrose + H2O → glucose + fructose
You have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!
b. Choose all true statements for enzymes below A) All enzymes are made up of amino acids. B) Enzymes can increase the equilibrium constant for a given reaction by a thousand-fold or more. C) Enzymes can increase the reaction rate for a given reaction by a thousand-fold or more. D) Their catalytic activity is independent of pH. E) They are generally equally active on R and S enantiomers of a given substrate. F) To be effective, enzymes must be present at the same concentration as their substrate. G) Enzyme activity is usually increased in the presence of denaturants like SDS and urea. H) Catalytic rate of enzymes cannot exceed what is dictated by the diffusion limit.
The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
For each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result. A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glucose to fructose. This reaction is catalyzed by a(n) (dehydrogenase, isomerase, kinase, phosphatase).

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