21. You want to maintain pH = 7.0 for an enzyme-catalyzed reaction that will producehydrogen ions along with the desired product. At equal concentrations, which weakacid, if any, will serve as the better buffer for the reaction: acid A, with pk₁= 6.5, oracid B, with pk=7.5?A) acid AB) Water is as good as either of the acids available.C) acid BD) Both are equally effective.

Here we are undertaking a reaction that will produce hydrogen ions (H+, generally termed as protons)…

Answered: You want to maintain pH-7.0 for an…

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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6. Enzyme X exhibits maximum activity at pH = 6.9. X shows a fairly sharp decrease in its activity when the pH goes much lower than 6.4. One likely interpretation of this pH activity is that: A) a Glu residue on the enzyme is involved in the reaction. B) a His residue on the enzyme is involved in the reaction. C) the enzyme has a metallic cofactor. D) the enzyme is found in gastric secretions. E) the reaction relies on specific acid-base catalysis. В
1.) A sample contains 0.003 mg of NaOH. How many micrograms (μg) is this? 2.) An experiment was performed in which 400 mL of 0.2 M urea was used. Calculate the number of millimoles (mmol) of urea contained in this sample. 3.) How many micromoles (μmol) of ATP are present in 4 mL of 5 mM ATP solution..
To characterize a purified enzyme, a biochemist has determined the reaction initial velocities, at various [S]。, using three different conditions: a) In the presence of the enzyme alone. b) In the presence of the enzyme and of a non-metabolizable substrate analog (compound A, at 150 µm). c) In the presence of the enzyme and of a compound that binds to the enzyme at a site different from that of the substrate (compound B at 60 µM). From his experimental results, he has drawn the Lineweaver-Burk plots (below). 1- Indicate which symbols (circles, triangles, diamonds) on the graph correspond to the experiments a, b, c. Justify your answer. 2- Determine graphically Km, Kmapp., Vmax and Vmaxapp. 3- Determine the inhibition constants Ki for the compounds A and B (i.e. the dissociation constants of complexes El). 1/V₁ (min.xM-¹) -6000 -4000 -2000 2.5 2 1.5 1 0.5 0 2000 4000 1/[S], (M-¹) 6000
Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…
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The enzyme urease is widely used for determining urea concentration in blood. The Michaelis constant for urease at room temperature is 2.0 mM and k2 = 2.8 × 104 s-1 at pH = 7.5. Based on the kinetic experiment, when 0.34 mM urease was used, the initial rate of the reaction was determined to be 3.49 M/sec. What is the concentration of urea in blood in unit of mM? Please keep your answer to two decimal place. Please convert all concentration unit to mM in calculation.
Explain how running a reaction with the enzyme aldolase at a pH of 14 affects its activity Enzyme Activity e Activity 765432TO Factors Affecting Enzyme Activity 0 6543 2 6 Solution pH 8 a) It significantly diminishes activity because enzyme is denatured b) It significantly diminishes activity because the enzyme becomes too reactive Oc) It will quadruple its activity because enzyme is denatured and free Question 9 (5 points) Estimate the optimum pH required for maximum enzyme activity 10 d) It will double its activity because enzyme now has more active sites 12 Factors Affecting Enzyme Activity
Which of the following is TRUE under the following conditions: the enzyme concentration is 2.5 nM, substrate concentration is 75 nM, the KM = 150 nM, and the Vmax = 20 nmol/min a) The rate of the reaction is 20 nmol/min! b) The rate of the reaction is between 10 nmol/min and 20 nmol/min. c) The rate of the reaction is 10 nmol/min. d) The rate of the reaction is below 10 nmol/min. e) The rate cannot be determined from the above information.
Describe how you would make the following solution containing two enzymes. 1 mL total volume in Buffer X with 10nM of enzyme A and 50nM of enzyme B You are given a solution of enzyme A at 1 mg/mL and a solution of enzyme B at 1 mg/mL. The molecular weight of enzyme A is 75,000 g/mol and the molecular weight of enzyme B is 130,000 g/mol.
For an enzyme kinetics experiment, a student prepared a reaction mixture by mixing 450 microliters of 0.75mM PNPP with 4.25ml of 0.2M Tris-HCl buffer. When he is ready to measure the absorbance, he added 0.3ml of Alkaline Phosphatase to the mixture and mixed thoroughly. What is the substrate concentration at the beginning of the reaction in mM ?
Sketch on one reaction rate vs. substrate concentration graph & sketch on one Lineweaver-Burk type plot the following:a) A Michaelis-Menten enzyme with a Vmax = 60 1/s and a KM = 125 M.b) An uncompetitive inhibitor of the enzyme described in a).c) An allosteric enzyme with the same Vmax as the enzyme described in a) and follows the sequential model
a) The equilibrium reaction for the aqueous dissociation of acetic acid is shown below. CH3COOH(aq) = CH3COO-(aq) + H+ (aq) Given the data in the table below and your knowledge of the "chemical standard state" (X) and the “biochemical standard state” (Xº'), answer parts a) to e). c) For the dissociation of acetic acid at 298.15 K, calculate AG and the corresponding pK₁. b) Even though by definition, AfG©(H+ (aq)) = 0 and_AƒGº¹(H+(aq)) = 0, these are different physical quantities. What precisely does each represent? Calculate at 298.15 K, AG' for CH3COOH(aq) and CH3COO¯(aq). Gibbs free energy of formation, in units of kJ mol-¹, at T = 298.15 K AfGe A¢G° -396.5 -369.3 0 CH3COOH(aq) CH3COO- (aq) H+ (aq) d) For the dissociation of acetic acid at 298.15 K, calculate ArGº¹. LOXF 0 Finally, using the formula to convert between standard states, show that that your calculated values of AG and A.Gº are in agreement. jonly this

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You want to maintain pH-7.0 for an enzyme-catalyzed reaction that will produce hydrogen ions along with the desired product. At equal concentrations, which weak acid, if any, will serve as the better buffer for the reaction: acid A, with pk-6.5, or acid B, with pk-7.5?