To characterize a purified enzyme, a biochemist has determined the reaction initialvelocities, 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 asite 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 tothe 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. thedissociation constants of complexes El).1/V₁ (min.xM-¹)-6000-4000-20002.521.510.50200040001/[S], (M-¹)6000

Enzymes are usually protein catalyst which catalyzes several biochemical reactions. Inhibitors (I)…

Answered: To characterize a purified enzyme, a…

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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To purify a given enzyme from a crude extract that contains it, fractional precipitations, exchange chromatography are successively tested ionic and exclusion chromatography, with the results shown in the following table: Volume of dissolution Protein concentration Enzymatic activity (ml) (mg/ml) (U/ml) a) Calculate the percentage of recovery of the enzyme after each of the manipulations to which it has been subjected. b) Indicate if it is necessary to continue purifying the enzyme or if it is expected to have reached its electrophoretic homogeneity.
In modern and recent application of a catalyst and an enzyme used in a chemical and biochemical reaction a) give the commercial or trade name of the catalyst and enzyme of both rxn b) the properties of the catalyst and enzyme (e.g., shape, size, colour, price).
An enzymatic reaction was carried out in a batch-operated reactor until exhaustion of the substrate. The formation of the product was monitored over time, obtaining the results shown in Table 1. Answer: a) Knowing that the initial substrate concentration was 0.2 M and that the stoichiometry reaction is: 1S –> 2P, estimate the substrate concentration over time from the data from [P] data in Table 1; b) Determine the parameters of the Michaelis-Menten equation, Vmax and Km, by fitting direct from the hyperbola function; c) Determine the parameters Vmáx and Km, by the linearized equation;
There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: (a) How do I run the experiment to find the kinetic properties of the enzyme, KMand Vmax? (b) The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.
There are six classes of enzymes, namely oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. (i) (ii) Cell disruption is one of the steps performed during enzyme production. Explain the reason of performing cell disruption in enzyme production and provide THREE (3) enzyme extraction methods for this type of enzyme. Explain the principles of gel electrophoresis as one of the methods used for enzyme purification.
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: The enzyme has optimum activities at 35oC. With the correct captions for X and Y axes, help me to draw:(a). A temperature profile graph, from 20 to 70oC.(b). Please explain the two ways how temperature can affect the enzymereaction.
Which of the following is true under the following conditions: an enzyme displaying Michaelis-Menten kinetics where the enzyme concentration is 10 nM, the substrate concentration is 45 mM, and the Km is 50 µM? a) The enzyme has low catalytic efficiency for the substrate. b)The rate of catalysis is near half-maximal velocity. c)The enzymatic reaction is near maximal velocity. d)Halving the substrate concentration has little effect on the catalytic rate. e) There is not enough information provided.
Consider the enzyme pancreatic amylase, which has an optimum pH of 7.0. How is the rate of a pancreatic amylase-catalyzed reaction affected by each of the following changes: (a) lowering the pH from 7 to 4; (b) increasing the pH from 7 to 9; (c) decreasing the temperature from 37 °C to 28 °C; (d) increasing the temperature from 37 °C to 50 °C?
s) In two experiments carried out in a research lab, an enzyme reaction is run with and without an inhibitor. Samples were taken over time to measure the concentration of product as the reaction proceeds, with raw data given below. Data were collected at 34 °C and pH 7.5, using [S] = 0.115 M (for both trials) & [E], = 0.0024 M (for both trials): Product concentration (mol P/L) No inhibitor [1] = 0.019 M 0 0 0.0011 0.0023 0.0031 0.0045 0.0074 0.0119 0.0195 0.0271 0.0410 0.0479 0.0550 0.0588 0.0600 Time min 0 3.5 9 13 17 26 43 69 104 156 208 311 415 519 0.0016 0.0038 0.0052 0.0078 0.0111 0.0180 0.0281 0.0412 0.0525 0.0587 0.0598 0.0600 0.0600 A. Determine the initial reaction velocities for both reactions. B. From these data, can you determine what type of inhibition is occurring? If so, show evidence of the type of inhibition occurring. If not, describe what experiment(s) should be done to determine the type of inhibition (competitive, non-competitive or uncompetitive), as well as how…
Two different preparations of the same enzyme are characterized below. Total protein (mg) Total activity (activity units) Step Volume Specific activity (ml) Preparation 1 300 1000 600,000 Preparation 2 200 1000 500,000 a) Fill in the 3 double-underlined blanks on the table below. b) Which of the 2 preparations would you think is likely to be more pure? Explain.
Indicate i) the class of enzymes to which it belongs to, ii) name the kind of bond that is modified due to its activity, iii) indicate the substrate that is recognised by the enzyme using the amino acid three letter code and iv) whether the enzyme displays high or low substrate specificity. Must be less than 50 words total.

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