Answer both questions A certain enzyme has a glutamic acid residue in its active site that is responsible for the enzyme's activity. However,any given enzyme will only be active if the side chain of this residue is deprotonated. At what pH will 99% of theenzyme molecules in a sample become active (i.e. what is the lowest possible pH required for 99% of the enzymemolecules to be active)? The pk of the side chain of glutamic acid is 4.3.Question 20Identify the N-terminal residue in the peptide below.N-CH-C-N-CH-C-N-H C.CHCH,CH*NHHN'-CH-H CH, H CH,ÇHčOOHHHH CH.H CH,SH

The explanation is given below-

Answered: A certain enzyme has a glutamic acid…

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.50E

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Sickle cell anemia is caused by a single mutation in the hemoglobin protein from a Glu to a Val, which results in which alteration in the hemoglobin subunits? A) more positive charges and formation of a hydrophilic contact point B) fewer negative charges and formation of a hydrophobic contact point C) fewer positive charges and formation of a hydrophobic contact point D) more negative charges and formation of a hydrophilic contact point E) more neutral charges and formation of a nucleophilic contact point
The time that is required for an enzyme to convert one substrate molecule into one product molecule is _________ A. Km. B. 1/kcat. C. 1/Km. D. kcat. Which of the following does not apply to the concerted model for subunit behavior: A. Each subunit can exist in a relaxed (R) and taut (T) conformation. B. All subunits will be in either the R or the T conformation at the same time. C. Some subunits can be in the R state while others are in the T state. D. The presence of inhibitors will lead to more of the enzyme being in the T form E. The presence of activators will lead to more of the enzyme being in the R form
Chorismate mutase is an enzyme that promotes a pericyclic reaction by forcing the substrate to assume the conformation needed for the reaction. The product of the pericyclic reaction is prephenate that is subsequently converted into the amino acids phenylalanine and tyrosine. What kind of a pericyclic reaction does chorismate mutase catalyze?
Which one will make the largest contribution to hydrophobic interactions via LDFs within the active site of an enzyme?
How does the near attack conformation (NAC) contribute to enzyme function?
3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?
A chemist wanted to test his hypothesis that the disulfide bridges that form in many proteins do so after the minimum energy conformation of the protein has been achieved. He treated a sample of an enzyme that contained four disulfide bridges with 2-mercaptoethanol and then added urea to denature the enzyme. He slowly removed these reagents so that the enzyme could re-fold and re-form the disulfide bridges. The enzyme he recovered had 80% of its original activity. What would be the percent activity in the recovered enzyme if disulfide bridge formation were entirely random rather than determined by the tertiary structure? Does this experiment support his hypothesis?
Because of its bat configuration, Batman's body produces excess nitrogen and excretes it as a form of urea, NH2CONH2. The reaction that produces it is the combination of arginine (C6H14N4O2) with the body's water to give urea and ornithine (C5H12N2O2), according to the following reaction: C6H14N4OR2 + H2O → NH2CONH2 + C5H12N2OR2 arginine urea ornithine a. Assuming Batman is a perfect (ideal) machine, his body completely removes the produced urea which is 95 mg of urea; calculate the mass of arginine that must have been used by his body. b. Calculate the mass of ornithine that his body produced. c. If the rest of normal humans are not a perfect machine, it has been established that for this case, the normal human produces 0.0003686 lb of ornithine. What is the reaction efficiency of the normal human body compared to Batman's.
Determine the branch points and reducing ends of amylopectin. A 0.5g sample of amylopectin was analyzed to determine the fraction of the total glucose residues that are branch points in the structure. The sample was methylated and then digested, yielding 50 μmol of 2,3-methylglucose and 0.4 μmol of 1,2,3,6-tetramethyl glucose. (MWglucose = 162 g/mol, minus H2O) What fraction of the total residues are branch points? How many reducing ends does the amylopectin have?
The charge form of the aspartic is believed to participate in a reaction catalyzed by an enzyme. At pH = 9.0, what is the probability that the aspartic acid will be charged?
1.) Did the lactase enzyme show specificity? Support your answer by comparing yor data for lactose and sucrose. 2.) How is the rate of enzyme-catalyzed conversion affected by temperature? Explain? 3.) How is the rate of enzyme-catalyzes conversion affected by acidity (ph) of the solution. Explain?
At 20°C, protein-Z binds DNA with a free energy of -7 kJ/mole. Protein Z has an unfolding free energy of 11 kJ/mole without ligand bound and 15 kJ/mole with ligand bound. Does the unfolded/denatured form of protein Z bind to DNA, and if so - what is the AG of binding of the unfolded form?

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