Si=0VOi=1i = 2.4i = 3.7v10.058v20.0440.4550.0750.950.1280.10.0811.3640.1680.1290.0992.2690.2220.1740.1343.6360.2720.2090.165.450.3110.240.1829.0910.3510.27 0.207s unit: mM, v unit: mM/min, i unit: mMv30.0360.0660.080.1080.130.150.167The ff: table showed data of enzyme catalytic reaction. The rate of reaction (v) decreased with the addition ofinhibitor. Differerent concentrations of inhibitor (f) were tested and the data showed that inhibition intensifiedas the inhibitor concentrations is increased. Find the ff:1. Find intercepts, slopes, Ks ^app, vmax ^app for inhibited reactions at all inhibitor concentrations usingLineweaver-Burk plot. Indicate if there are no changes.

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

Answered: The ff: table showed data of enzyme…

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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An inhibitor "I" is added to the enzymatic reaction at a concentration of 1.0 g/L. The data obtained are shown in the table below. No Inhibitor With Inhibitor [S](g/L) v ([E0] = 0,015 g/L) (g/L.min) v ([E0] = 0,015 g/L)(g/L.min) 40 2,28 1,818 20 1,74 1,316 13,4 1,4 0,986 10 1,18 0,76 8 1 0,62 (a)What kind of inhibition occurred?(b)Determine Ki (in g/L) for the inhibition of the previous exercise.
If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.
5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142
Graph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.
In Lineweaver Burk plot: O a. The slope of the plot is the Vmax/Km O b. The intercept on X-axis is 1/Km. O c. The intercept on y-axis is 1/Vmax O d. double-reciprocal plot of enzyme kinetics is generated, where 1/VO is plotted as a function [S]. O e. All answers are correct
The figure below shows the dependence of the enzyme's rate, v (in µM/min), as a function of substrate concentration, S (in mM). Also shown is the dependence of the rate in the presence of an inhibitor, present at a concentration of 0.2 mM. Based on this information, which of the following does this inhibitor most likely interact with? 1/v 1- 05 1/[S) O A. Michaelis complex O B. [E O C. free enzyme O D. free substrate O E. Both "A" and "B."
please help me understand this practice problem with as much details as possible. An enzyme reversibly binds a substrate. The rate constant (kcat) for catalytic conversion of enzyme- substrate complex into product and free enzyme is 1.0 s-1. The rate constant for dissociation of enzyme- substrate complex (k-1) is 9.0s^-1. 1) For each substrate binding event, what is the probability that substrate is converted into product rather than dissociated without conversion? 2) What is the probability that 20 consecutive binding events result in no product formation? 3) If you evaluated 1,000 different sets of 20 consecutive binding events, what would be the average number of product molecules formed (per 20 binding events)? 4) What is the probability that 20 consecutive binding events result in a number of product molecules at least equal to this average?
Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…

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