In the Lineweaver Burke plot shown below, which of the following is true?With inbitoWthout nhitorO Km is increasing. Vmax is decreasingKm is decreasing, Vmax is decreasingKm is increasing, Vmax is increasingKm is decreasing, Vmax is inQUESTION 35As per the Enzyme commission classification, the tranferases belong to which of the following Class?O 2O 4O 3Click Save and Submit to save and submit. Click Save All Answers to save all answers.78 F Mostly cloudy

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Answered: In the Lineweaver Burke plot shown…

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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Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
Which of the following are true when enzymes and substrate interact? kı E + S ● ES- -P k-1 the rate of the formation of ES = k1 [ES] the rate of the formation of the product = k2[ES] k1 [ES] = k-1 [ES] the rate of breakdown of ES to reform the enzyme and substrate = K-1[E][S] the rate of formation of ES = k1[E][S]
On the figure below are shown three Lineweaver-Burk plots for enzyme reactions that have been carried out in the presence, or absence, of an inhibi- tor. Indicate what type of inhibition is predicted based on each Lineweaver- Burk plot. For each plot indicate which line corresponds to the reaction without inhibitor and which line corresponds to the reaction with inhibitor present. 1 1 1 [S] [S] [S]
k_1 E + SES E + P +0 k₂ S ↓↑ KIS ESS Based on this model, please answer the following questions: i) This is the model for what? Uncompet tive ii) Show the rate equation for an enzyme reaction of this type. iii) Show the Lineweaver-Burk plot for this case. A
Given the following enzyme catalyzed reaction, identify the class and subclass of the enzyme involved: %3D CH3CH CH,CH2 SCOA SCOA COO СО
Given the following reaction, identify the class and subclass of the enzyme involved. H. CH2OH H-C-OH C=0 но-с-н но-с-н H-C-OH H-C-OH H-C-OH H-C-OH CH2OPO,2 CH2OPO,2- Class: [ Select] [ Select ] Ligase Hydrolase Lyase Subcla Transferase Isomerase Oxidoreductase
Studies were carried out to investigate some kinetic properties of alkaline phosphatase (ALP) extracted from Lepus townsendii liver. Incubation of ALP extract with 4- nitrophenylphosphate (4-NPP) formed the basis for determination of enzyme activity. Spectrophotometric method was used to assay the enzyme activity, and the kinetic constants- maximum enzyme velocity (Vmax) and Michealis-Menten constant (Km) were evaluated. Figure 2 shows the Lineweaver-Burk plot of ALP assay in the presence of inhibitor NaH;PO4 (0) and the control (+) analysis. [I]: concentration of inhibitor = 0.67 mM. 1/V, uM*min x 104 40- 30 20 y-Intercept 10 x-intercept -1/K. (1+ [1]/K)/ 12 1/[S)x 102 (M) Figure2 (i) Estimate Km and Vmax in the absence and presence of the inhibitor. (ii) What is the type of inhibition illustrated by the inhibitor? Explain.
Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1
Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate  delta delta G〒 on your sketch: Chemical step is rate limiting
The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
Please note the reaction expression below. Which of the following rate constants describes the breakdown of the enzyme-substrate complex? There may be more than one answer. k₂ E+S OK-2 U k₂ 0 k₁ OK.1 k3 k.3 SES EPE+P K.3 K.₂ k.

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In the Lineweaver Burke plot shown below, which of the following is true? Wth inhto Wthout inhittor Km is increasing. Vmax is decreasing Km is decreasing, Vmax is decreasing Km is increasing, Vmax is increasing Km is decreasing, Vmax is increasing