The Lineweaver-Burke plot was originally developed in order to "linearize" the dataobtained from enzyme kinetics experiments, in order to facilitate the determinationof kinetic parameters. Why is it not considered to be an accurate method for thispurpose?It is very difficult to draw a straight line on a computer.It is very difficult to calculate the variables required for the "x" and "y" axis.It is more accurate to use the standard "V versus [S]" plot to determine Vmaxand KM-The plot weights the least accurate data points the most heavily.It is no longer considered to be acceptable to extrapolate from known data.

For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Answered: The Lineweaver-Burke plot was…

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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A TAMU undergraduate biochemistry student is tasked with characterizing a new enzyme. After devising an assay, the student does some initial experiments. When initiating the reaction by adding the enzyme to a solution of substrates (but no products) she finds that at the earliest times the change in the [A] is non-linear and increasing and then becomes linear for awhile and then decreases eventually to zero. Explain what is unusual and what various aspects of the time course mostly likely means.
The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.
During successful purification of every enzyme, the following may be expected: Select ALL that apply. 1. Solubility in NaCl increases 2. The activity increases 3. The specificity increases 4. The number of subunits increases 5. the epitope number increases
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…
Please describe the information on transferase and draw its Michaelis-Menten Plot and annotate Km and Vmax in the graph.
A pyrene/kumarin FRET pair (ro=39 A)) was used to study the structural change of the enzyme during the reaction. Computer calculations show that this pair is (35 A)) away from one heteromorphic body and (46 A )) away from the other. What is the difference in FRET efficiency between the two dimples?
Chymotrypsin is an enzyme that is optimized to function in the small intestine (at a pH of ~7.4). Explain, given what you know about the chymotrypsin mechanism and what we learned about acid/base chemistry, why chymotrypsin would not be able to initiate catalysis if it were secreted into the stomach (pH ~2.5).
The purpose of the progress curve is to determine if an enzymatic reaction rate remains constant for given concentrations of enzyme and substrate, for a given assay time (20 min). How long did the rate of reaction of WGAP remain constant in your experiments? How do you know? What would cause the reaction rate to not be constant and plateau after some time?
Table 1. Kinetic parameters of a chosen model wild-type (WT) enzyme and three catalytically-improved mutants (M1 to M3). Enzyme variants k (8¹) WT MI M2 M3 50 500 1000 50 K₁, (μM) 10 100 100 1 k/K (HM¹¹ s¹) 5 The study above was done on a wildtype enzyme and three genetically-engineered mutants. The purpose was to find a mutation to improve the catalytic efficiency of the enzyme for industrial use. Which is the most accurate statement concerning the data? M2 is the optimal choice when substrate concentrations are saturating. The wildtype enzyme is still preferable to M3 when S<
Two therapeutics, methotrexate and fluorouracil, inhibit the formation of dTMP, at different points in the synthesis. One is a suicide inhibitor and one is a competitive inhibitor. a. What therapeutic applications are there for inhibiting the synthesis of dTTP? (ie. What are they treating?) b. Identify the which molecule is the competitive inhibitor and which one is the suicide inhibitor and explain how you know.
The Nutrition Facts label on most food products shows % daily values based on a food energy requirement of 8,360 kJ (2,000 kcal) at normal resting state. a) Assuming that the efficiency of converting food energy to ATP is 50%, calculate the mass of ATP (in kg) that is harvested daily by the human body from 8,360 kJ of food energy. A total of 30.5 kJ of energy is needed to synthesize one mole of ATP under standard conditions. The molar mass of ATP is 505 g/mol. b) For an average 68-kg (150 lbs.) human adult, calculate the % mass of extracted ATP (from your answer in 2a) relative to body weight.
Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1. What would be the Vmax in units of mole s^-1?

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