CHEM151/251Biochemistry 1a. Determine Km1. The following data were obtained for a competitive inhibition study in which the [I] = 3 µM for eachdetermination of vo in the presence of inhibitor. The Vmax = 200 μM P/min for both data sets.200Vo (UM P/min)8 8 8 8 8 8 8 8 818016014012010040Name (Print)/ID #:the absence of inhibitor.Participation Question # 10No Inhibitor50+Inhibitor100[Substrate] (UM)150b. Determine Km, app for the data obtained in presence of inhibitor.200c. Calculate the value for Ki. Note: a = 1 + [I]/Ki and a¹ = 1 + [I]/Ki*.for the data obtained in

In competitive inhibition, only the apparent Km is affected (Km,app> Km),The Vmax remains…

Answered: 1. The following data were obtained for…

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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1. Start with the Michaelis-Menten equation and convert it to a double-reciprocal equation. Show how you would make a linear Lineweaver-Burk plot using this equation. 2. Based on th chart make a Lineweaver-Burk plot and later use the plot to complete the information in the table.
2. An enzyme-catalyzed reaction is carried out at several different substrate concentrations (listed below), either (1) with no inhibitor, or (2) in the presence of an inhibitor, I, at 0.63 g/L. Given the following data, determine: A. what type of inhibitor I is B. the value of Ki No Inhibitor: With Inhibitor: Substrate Concentration (g/L) 0.86 Reaction Velocity (g/L-s) Reaction Velocity (g/L-s) 0.179 0.161 2.35 3.80 4.90 6.10 18.4 0.398 0.567 0.666 0.726 0.950 0.322 0.407 0.443 0.495 0.639
graph the data from the table after taking recipocals of [S], V without inhibitor and V with inhibitor. It should be Lineweaver - Burke. use graph paper or excel. however upload graph and answers as 1 document as jpeg, pdf, or word. there should be 2 lines on 1 graph and both lines should cross the Y axis and hit the X axis (negative X axis). label both axes, determine Km and Vmax (show work) in the presence and absence of inhibitor State type of inhibition and if inhibitor resembles the substrate or not. can more substrate relieve the inhibition? [S] (UM) 3 10 30 5 90 Velocity (umol minute-¹) No inhibitor 10.4 14.5 22.5 33.8 40.5 Inhibitor 4.1 6.4 11.3 22.6 33.8
Calculate the concentration of p-aminophenol control to match the 0.075 % w/w limit in 200 mg/10 ml Your Answer: 0.0015% show work
Which of the following is true about a mixed type inhibition? a. None of these is true b. A Lineweaver-Burk plot will give parallel lines c. The lines of a Lineweaver-Burk graph will cross in the top left quadrant d. The KM will change but not the Vmax
4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.
Given the parameters below:1. u(max) = 1.0/ h Ks = 10 uM2. u(max) = 0.7/h Ks = 2 uM) a. sketch the comparative Substrate Concentration vs.u(max) graphs for 1. b. sketch the comparative Substrate Concentration vs.u(max) graphs for 2. (answer a and b)
4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM
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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