Our assay had two reactions, one catalyzed by glucose oxidase, and the second by peroxidase. What must be true about the maximum possible rates (Vmax) ofthe two enzymes to insure that the velocity we measure corresponds to glucose oxidase activity, and not peroxidase activity?BIUSX' X. 14-AMI

Enzyme kinetics assays (or simply Enzyme assays) are carried out to determine the kinetic parameters…

Answered: Our assay had two reactions, one…

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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J. C. Servaites, in Plant Physiol. (1985) 78:839–843, observed that Rubisco from tobacco leaves collected before dawn had a much lower specific activity than the enzyme collected at noon. This difference persisted despite extensive dialysis, gel filtration, or heat treatment. However, precipitation of the predawn enzyme by 50% (NH4)2SO4 restored the specific activity to the level of the noon-collected enzyme. Suggest an explanation.
If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? 0.125 mM 0.25 mM 0.50 mM 1.25 mM 5.0 mM
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. Based on the following reaction expression, what is the Km value for this enzyme? E+SESE + P . . . k₁ = 880.8 M-¹5-1 k.₁ = 42.18 S-1 k₂ = 56.29 S-1
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
What ion or ions are required for PYC activity? What ion or ions inhibit PYC activity? Remember, Mg2+ is the control substance, and not expected to have any effect on the enzyme’s activity.
If you want to determine the KM for lactate, what protocol do you set up? Discuss the significance of the following kinetic parameters that are used to characterize enzyme activity: KM, Vmax, kcat, and kcat / KM.
Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-¹. Table 1: Glucoamylase Activity at different temperatures Maltodextrin Concentration (μmol/L) 0.5 1 1.5 2.2 5.5 11 Initial Reaction Velocity (μmol/L.s) T = 40°C 2.1 3.5 4.9 5.6 589 8.3 9.3 T = 60°C 5.2 9.7 13 16 23 31
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.
An uncatalyzed reaction progresses at a rate of 20micromoles per minute while the same reaction in the presence of an enzyme progresses at a rate of 100micromoles per second. What is the rate enhancement achieved by the presence of the enzyme? At 25oC, how much energy is required to produce a 10-fold rate enhancement? At the same temperature, how much energy is required to produce a million-fold rate acceleration?
The following data have been obtained for two different initial enzyme concentrations for an enzyme-catalyzed reaction. [E]=0.015 g/l) (g/l-min) [S] (g/l) v([E]=0.00875 g/l) (g/l-min) 1.14 20.0 0.67 0.87 10.0 0.51 0.70 6.7 0.41 0.59 5.0 0.34 0.50 4.0 0.29 0.44 3.3 0.39 2.9 0.35 2.5 a. Find K b. Find V for [E]=0.015 g/l. c. Find V for [E]=0.00875 g/l. d. Find k2. Use Eddie-Hostee plot to find your answer. Compare your result using Hanes- Wolf plot.
1) Is the ratio of the forward rate constant and reverse rate constant changed by the presence of an enzyme catalyst? 2) 4) What is the simplest mathematical relationship between substrate concentrations [S], initial velocity (Vo) of an enzyme catalyzed reaction, the maximal velocity of the reaction (Vmax), and the ½ maximal Vo (i.e. Km) ? (Hint: what is the Michaelis-Menten Equation? 3) Graphically illustrate the most useful derivation of the Michaelis-Menton equation (that darn linearized, double-reciprocal)
E. coli oriC is rich in A · T base pairs. Why is this advantageous?

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Our assay had two reactions, one catalyzed by glucose oxidase, and the second by peroxidase. What must be true about the maximum possible rates (Vmax) o the two enzymes to insure that the velocity we measure corresponds to glucose oxidase activity, and not peroxidase activity?