7-52An experiment is performed to test a suggested mechanism for anenzyme-catalyzed reaction.The results fit the model exactly (towithin experimental error). Do the results prove that the modelis correct? Why or why not?

INTRODUCTION : Enzyme : Enzymes are proteins which act as biochemical catalysts by accelerating or…

Answered: An experiment is performed to test a…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 20P

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8 of 15 An enzvme has an all-important histidine residue in its active site such that substitution with an other amino acid would result to the loss of catalytic activity. What are the possible mechanisms by which this histidine residue may facilitate catalysis? I. Acting as proton acceptor. II. Forming of covalent bond with the substrate via an ester bond. III. Serve as stabilizer of electrophilic substrate because of its nucleophilic character. Select the correct response: land II Il and III land IlI I. Il, and III
The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5 respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these 2 amino acid residues explain the pH-activity profile of lysozyme?
A16 Compound A is the substrate for two enzymes, E, and E2, involved in the synthe- sis of an amino acid and an antibiotic, respectively. Their reaction rates, r, and r2, at an arbitrary concentration of E, and E, were measured at different concen- trations of A. However, the data were not labeled properly (shown in Table P.4.1), and the student who did the measurement needs help to sort out which dataset is for E,. Determine the K and rmax for both enzymes, with respect to the concen- tration of A. Which set of data is more likely to be for E, and which for E, and why? Table P.4.1 Reaction kinetics of a common substrate A for two enzymes. Concentration of 0.2 0.6 1.2 3. 4 5 8 9 12 15 A (mM) Reaction rate (r.) (mmol/L'min) Reaction rate (r,) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
1 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…
P3D.2 In biological cells, the energy released by the oxidation of foods is stored in adenosine triphosphate (ATP or ATP“).The essence of ATP's action is its ability to lose its terminal phosphate group by hydrolysis and to form adenosine diphosphate (ADP or ADP): ATP* (aq) + H,O() → ADP* (aq) + HPO (aq) + H,O*(aq) At pH = 7.0 and 37°C (310K, blood temperature) the enthalpy and Gibbs energy of hydrolysis are A,H =-20kJ mol and A,G=-31 kJ mol", respectively. Under these conditions, the hydrolysis of 1 mol ATP“(aq) results in the extraction of up to 31kJ of energy that can be used to do non- expansion work, such as the synthesis of proteins from amino acids, muscular contraction, and the activation of neuronal circuits in our brains. (a) Calculate and account for the sign of the entropy of hydrolysis of ATP at pH = 7.0 and 310K. (b) Suppose that the radius of a typical biological cell is 10µm and that inside it 1x 10ʻ ATP molecules are hydrolysed each second. What is the power density of…
A16 Compound A is the substrate for two enzymes, E, and E, involved in the synthe- sis of an amino acid and an antibiotic, respectively. Their reaction rates, r, and r, at an arbitrary concentration of E, and E, were measured at different concen- trations of A. However, the data were not labeled properly (shown in Table P.4.1), and the student who did the measurement needs help to sort out which dataset is for E,. Determine the K, and rmax tration of A. Which set of data is more likely to be for E, and which for E,, and why? for both enzymes, with respect to the concen- Table P.4.1 Reaction kinetics of a common substrate A for two enzymes. Concentration of 0.2 0.6 1.2 3 4 6. 8 9. 12 15 A (mM) Reaction rate (r.) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 .88 4.9 4.92 4.94 4.95 4.96 4.97 Reaction rate (r,) (mmol/L*min) 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
A synthetic substrate, the para-nitrophenylacetate (PNPA), is used to monitor enzyme activity of protein P. The product of the hydrolysis reaction absorbs at 410 nm with a molar extinction coefficient of 4 000 M-¹.cm-¹. 1- Write the reaction catalyzed by the protease P using the pNPA substrate. 2- The enzyme extract is too concentrated and a 1/300 dilution is needed for enzyme tests. Considering that you would need at least 600 µL of diluted enzyme extract for activity tests, indicate which volume of buffer and enzyme extract you must use for the dilution.
A16 Compound A is the substrate for two enzymes, E, and E, involved in the synthe- sis of an amino acid and an antibiotic, respectively. Their reaction rates, r, and r2, at an arbitrary concentration of E, and E, were measured at different concen- trations of A. However, the data were not labeled properly (shown in Table P.4.1), and the student who did the measurement needs help to sort out which dataset is for E,. Determine the K and rmax for both enzymes, with respect to the concen- tration of A. Which set of data is more likely to be for E, and which for E,, and why? Table P.4.1 Reaction kinetics of a common substrate A for two enzymes. Concentration of A (mM) 0.2 0.6 1.2 2 4 6. 8 9 12 15 Reaction rate (r,) (mmol/L'min) Reaction rate (r.) (mmol/L*min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
To approximate the concentration of enzymes in a bacterial cell, assume that the cell contains equal concentrations of 1,000 different enzymes in solution in the cytosol and that each protein has a molecular weight of 100,000. Assume also that the bacterial cell is a cylinder (diameter 1.0 μm, height 2.0 μm), that the cytosol (specific gravity 1.20) is 20% soluble protein by weight, and that the soluble protein consists entirely of enzymes. Calculate the average molar concentration of each enzyme in this hypothetical cell.
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
What features distinguish enzymes that undergo allosteric control from those that obey Michaelis-Menten equations? Give 2 differences
Lysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3D

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An experiment is performed to test a suggested mechanism for an enzyme-catalyzed reaction. The results fit the model exactly (to within experimental error). Do the results prove that the model is correct? Why or why not?