Macmillan LearningN.XConsider the data collected for an enzyme-catalyzed reaction.% (mM-s¯¹)0.370.832.223.08F2Determine Vmax and Km for this reaction.# 3#EDVmaxKm -F3[S] (mM)0.200.502.004.00JANMAN!$4PERNIERF3.08IncorrectV14-IncorrectFA%5TGBHOL6F5YH&7NF6UJ8DELLF7NK9F8O>F9PWF10{?[1F11}1F12BackspaceEnterShiftInsertPrintScreenDeleteHomeScrollLockEndⒸ Attempt 18:26 PM10/15/2023+PgUpPauseBreakPgDnmM-s-lmMGNumLock7Home481EndST5O

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

Answered: Macmillan Consider the data collected…

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 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…
D 1. 0.25 Short answer questions, write answers on blank paper. A plot of enzyme activity with and without an inhibitor present gave the following plot. 0.2 0.15 1/V v in mM/s 0.1 0.05 0 0 0.05 0.1 y=0.67x+0.02 0.15 y=0.2x+0.02 0.2 0.25 0.3 1/[S]. [S] in mM Without the inhibitor, what are the values of Vmax and Km? In the presence of the inhibitor, which of these items has changed and what is (are) the new value(s)? What type of inhibitor is present (explain why you have arrived at this conclusion)? Be sure to include units as necessary--answers that do not contain required units will be marked incorrect
Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical reaction catalyzed. 9. The living cell is the site of tremendous…
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
Name: Sincere Frias Date: (0/2/2od0 Period Ced th nzy ck. Enzyme Models & Factors Affecting Enzyme Action PART I – Lock and Key Model st In this part you will construct models of enzymes. Remove the last page and cut all shapes out. 2. The different shapes will represent both enzymes and substrates. 3. Match up as many of the pieces as you can. 1. Questions 1. The enzyme maltase combines the substrates h ydrolysis + Starch molecule to produce the disaccharide maltose. 2. The enzyme ATPase combines the substrates_molecule and to produce the ATP (Adenosine TriPhospate). Iriglyceride 3. The enzyme lipase works on the substrate called 4. The enzyme phosphatase works on the substrate called 5. What is the relationship between the substrate and the enzyme?
moodle.aaup.edu/mod/quiz/attem MISTRY I Section1 Lecture (20202_100213 purses / BIOCHEMISTRY I Section1 Lecture (20202_100213111 AAUP - JENIN) / 1 May -7 May Time left 0:37: Which of the following is not true for isozymes? O a. Many enzymes occur in several molecular structures called isozymes O b. Isozymes are enzymes that have a different other allosteric site O c. Various isozymes are expressed in different tissues of the body O d. Different isozyme catalyze the same chemical reactions, but differ slightly in their primary sequence and kinetic properties Next page pril 26 (Glycolysis, plysis Control + genesis Part I) Jump to...
S Savvas EasyBridge IS Savvas Realize asrealize.com/assignments/viewer/classes/61227fd32e855b44e0a77ded/assignments/96054946a5024ac29d3c30068e59b062/contents/c ming of Enzymes nzymes Drag each substrate to the enzyme with the matching active site. Enzymes 1. Changing environmental conditions, such as temperature or pH, can affect enzyme shape. How would this alter the enzyme's function? Substrates Type your answer here. acer
ANN/ SUAMF 2. (a) Fig. 2.1 shows the effect of temperature on the activity of enzyme E. rate of activity/ arbitrary units 40 60 80 100 temperature/C Fig. 2.1 () State the optimum temperature for enzyme E (i1) Suggest a possible identity for enzyme E, where it is found, and its function. identity of enzyme E where it is found function on the activity of another enzyme, F
Q1. We plan a farge scale purification of enzyme using a packed colum of polyacrylamide beads. We obtain the following data, in a bed. of volume. 201t Volume Eiuted (iters) ‘Concentration (Arbitrary Units] 126 00073 40 00162 (maximum) Find the yieid at 150 lites eluted.
An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
Time 3/33 answered Ở Show Hewtty, Carlos Remaining Please save all answers. Questions that you save can still be edi pu have 1 UNSAVED ANSWER- SAVE ALL ANSWERS Question 32 The initial rate for an enzyme-catalyzed reaction has been determined at several substrate concentrations. Data are as follows: The Km value (µM) is: TT [S] umol/L v[(umol/L) min-1] 22 10 39 20 65 50 102 100 120 200 135 Select an answer and submit. For keyboard navigation, use the up/down arrow kéys to select an answer. a 800 100 1200 2000 e 90 10
asrealize.com/assignments/viewer/classes/61227fd32e355544e0a77ded/assignr ng of Enzymes nzymes Effects of Enzymes This graph shows the effects of an enzyme on a particular reaction. The red line on the graph shows the reaction without the enzyme while the blue line shows how the reaction progresses with the enzyme. 2. According to the graph, the enzyme V Choose... affect the initial energy of the reactants. The enzyme V Choose... the activation energy. The overall energy released Check Answer

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Macmillan Consider the data collected for an enzyme-catalyzed reaction. % (mM-s-¹) 0.37 0.83 2.22 3.08 [S] (MM) 0.20 0.50 2.00 4.00 Determine Vmax and Km for this reaction.