If the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible? /content/0/HW%202-EnzymMichaelis Menten Plot.xls [Compatibility Mode] - MicrosoHomeInsertPage LayoutFormulasDataReviewViewAdd-InsAcrobat% CutCalibri- 11A AWrap TextGeneral自 CopyPasteBIUE } E I Merge & Center$- %$68 00Conditional FormiFormat PainterFormatting as TablClipboardFontAlignmentNumberC20fxFGJK.M1 [Ethanol]VoCalc. Vo delta^20.0070.060.020242 0.0015810.353.0.0150.110.0403570.004850.340.0310.160.073219 0.0075310.0680.210.125236 0.0071850.256.0.10.230.1547040.005670.20.280.206272 0.0054360.2• Vo8.0.30.290.232056 0.003358-Calc. Vo0.159.0.40.280.247526 0.0010550.036664100.111Km0.112Vmax0.3094070.0513140.10.20.30.40.516171819Fig. 9. Michaelis-Menten Plot using a value of 0.1 mM for Km.

Km is Substrate concentration at half Vmax. It can be calculated from Michael's Menton plot or lb…

Answered: f the new higher KM value is 0.1 mM…

f the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible?

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

See similar textbooks

Related questions

Q: Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal…

A: According to our guideline we can answer only the first three subports of the first question. So…

Q: Match the different names for inhibition mechanisms (1-5) with a description of their properties…

A: An inhibition mechanism refers to the process by which a substance or molecule, called an inhibitor,…

Q: You are trying to come up with a drug to inhibit the activity of an enzyme thought to have a role…

A: In competitive inhibition, an inhibitor molecule interferes with the binding of normal substrate to…

Q: On the graph provided, sketch a plot of Vo/Vmax vs. [S] for an allosteric enzyme, 1.0 0.8 0.6 0.4 02…

A: Allosteric enzymes are a class of regulatory enzymes which increases or decreases catalytic…

Q: You are trying to come up with a drug to inhibit the activity of an enzyme thought to have a role…

A: Km (also known as Michaelis constant) is the substrate concentration that allows the enzyme to gain…

Q: The graphs 3 and 4 representing 1/Vo = f(1/[S]。) have been done in the presence of a competitive…

A: Enzymes carry out most of the processes required for life. They are protein in nature and carry out…

Q: a protein collected through affinity chromatography displays no activity even though it is found to…

A: Protein is made up of one or more amino acids that are linked together to form a chain. The building…

Q: Enzyme Combination - Cla I + EcoRI What is the number of fragments? What are/is the size(s) of…

A: The restriction endonuclease are specific enzyme that are responsible for cutting double strength…

Q: Lineweaver Burk plot to determine the Vmax and Km

A: The Lineweaver-Burk plot, also known as the double reciprocal plot, is a graphical representation of…

Q: Latrotoxin identify the species which releases the toxin (if it is man-made then this will be all…

A: A latrotoxin is a neurotoxin with a large molecular mass discovered in the venom of spiders of the…

Q: rformed a lactate dehydrogenase (LDH) assay multiple times e same. This graph shows the results…

A: An enzyme is a protein which is required for carrying out a particular chemical reaction inside the…

Q: The table below summarizes the results of three kinetic experiments using the same enzyme and…

A: The double reciprocal curve is used to linearize the Michaelis-Menten curve to obtain the exact…

Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…

A: Enzymes are biological catalysts that help chemical processes occur faster. Enzymes are proteins…

Q: Consider the graph below. Reaction rate (v) Vmax 0 Effector 3 mM Effector 1, mM Control 0 mM Ko.5…

A: Enzymes are biological catalysts that increase the rate of biochemical reactions.Most enzymes are…

Q: Given the active site and reaction mechanism, identify the mechanism of irreversible inhibition for…

A: Irreversible inhibition is a process in which inhibitors bind covalently or non-covalently to a…

Q: ISP+OCZY+/F' I*P*O*ZY™ Lacz No IPTG IPTG LacY No IPTG IPTG

A: The Lac operon is a well-studied example of gene regulation in bacteria. It is an inducible operon,…

Q: 3. To the right is a Lineweaver-Burk plot for enzyme X along with two additional lines from testing…

A: Michaelis Menten constant for enzymatic activities, is a concentration of a substrate which is…

Q: In mixed inhibition as shown below, please draw a lineweaver-burk plot when Kl is greater than KI'.…

A: Michalis Menten equation for given reactionE + S ESE+PVo - Initial velocity or initial reaction…

Q: -Inhibitor +Inhibitor [S] (mM) V0&νβσπ; (μmol/sec). V0&νβσπ:&νβ σπ: (μmollsec) 0.0001 33 17 0.0005…

A: Km of an enzyme is the substrate concentration at half Vmax. It can be calculated from lb plot by…

Q: -Inhibitor +Inhibitor _[S] (mM) νο&νβσπ:(μmol/sec) ν0&νβσπ; &νβσπ;(μmol/sec) 0.0001 33 17 0.0005 71…

A: From the given data, I have calculated 1/S and 1/V0 in absence and presence of inhibitor. The plot…

Q: Drag the terms on the left to the appropriate blanks on the right to complete the sentences. Terms…

A: Nucleotide metabolism is the set of biochemical reactions that involve the synthesis and breakdown…

Q: (d) From your plot, calculate the activity of the enzyme. Use the space below to show your workings:

A: Enzyme kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction rate…

Q: Between the following 4 Km values, select the one that indicates binding of the enzyme to its…

A: Km is the concentration of substrate at which the enzyme achieve half Vmax.

Q: Compare the KM and Vmax of the enzyme in the absence and presence of inhibitors to determine what…

A: Inhibitors are the molecules which decrease the efficiency of enzyme activity.

Q: Consider the given data for an enzyme-catalyzed reaction. Determine the Vm, Km and the type of…

A: Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…

Q: What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is…

A: The relationship between Km and substrate concentration is that Km corresponds to the substrate…

Q: An extract of rat liver was prepared by homogenizing 65 g of tissue in 55 mL of buffer (Fraction 1).…

A: Given details in the problem: Fraction 1 is the initial fraction. Initial specific activity = 11.5…

Q: Why does the apparent KM decrease in the presence ofan uncompetitive inhibitor?

A: An enzyme inhibitor is a molecule that binds to enzyme and decreases its activity. By binding to the…

Q: Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to…

A: Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…

Q: What is the definition of 1 unit of Taq polymerase activity according to a commercial supplier of…

A: Taq polymerase is a thermostable DNA polymerase I and is isolated from the thermophilic eubacteria…

Q: An enzyme is mutated such that the KM of the mutated enzyme is lower than the KM of the original…

A: The objective of the question is to understand the effects of a mutation that lowers the KM of an…

Q: A junior student performed an experiment to found Ki values for 3 different competitive inhibitors.…

A: Competitive inhibitor competes for the same site to which the substrate binds on enzyme. Competitive…

Q: Why does a pure noncompetitive inhibitor not changethe observed KM?

A: The non-competitive inhibitor is a molecule that does not compete with the substrate to get bind to…

Q: what concentration of a competitive inhibitor is required to yield 60% inhibition of an enzyme at a…

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

Q: draw and label a Michaelis-Menten plot showing the effect of a compentitive inhibitor

A: Two scientists named Leonor Michaelis and Maud Leonora Menten, proposed a model which is known as…

Q: 3. Researchers purified a new enzyme and during an initial characterization determined the Vmax to…

A: Enzyme inhibition is when an inhibitor bind to the enzyme at the active site or another site, which…

Q: In pure noncompetitive inhibition: a. Where on the enzyme does the inhibitor bind? b. Does…

A: Enzymes refer to the protein that acts as a catalyst for the biochemical reaction. It facilitates…

Q: つく 146 Bb 9146 Bb 10311 Class E Etsy Traps E Traps New Free Chat + ☆ 口出…

A: Turnover number refers to the number of substrate molecules that is converted to the product…

Q: What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme…

A: Chymotrypsin is a proteolytic enzyme secreted by the pancreases in the small intestine.

Q: Please describe the information on transferase and draw its Michaelis-Menten Plot and annotate Km…

A: Enzymes are 3D tertiary globular proteins that function as reusable biological catalysts. Enzymes…

Q: 200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is…

A: In biochemistry and molecular science, enzyme purification is an essential process that isolates…

Q: For the following problem, indicate whether enzyme is repressed (-) or produced (+). Please show all…

A: The lac operon is a set of genes that are used in the metabolism of lactose in E. coli. The operon…

Q: i) Explain the pH dependence of lysozyme catalysis shown in the Figure 1 below 100 50 4 8. 10 pH…

A: Lysozyme It is enzyme which is found in secretions of body like tears, mucus, saliva, etc. This…

Q: the maximal velocity of the reaction the Km value of the uninhibited reaction the Km value of the…

A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Question

If the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible?

/content/0/HW%202-Enzym
Michaelis Menten Plot.xls [Compatibility Mode] - Microso
Home
Insert
Page Layout
Formulas
Data
Review
View
Add-Ins
Acrobat
% Cut
Calibri
- 11
A A
Wrap Text
General
自 Copy
Paste
BIU
E } E I Merge & Center
$- %
$68 00
Conditional Formi
Format Painter
Formatting as Tabl
Clipboard
Font
Alignment
Number
C20
fx
F
G
J
K.
M
1 [Ethanol]
Vo
Calc. Vo delta^2
0.007
0.06
0.020242 0.001581
0.35
3.
0.015
0.11
0.040357
0.00485
0.3
4
0.031
0.16
0.073219 0.007531
0.068
0.21
0.125236 0.007185
0.25
6.
0.1
0.23
0.154704
0.00567
0.2
0.28
0.206272 0.005436
0.2
• Vo
8.
0.3
0.29
0.232056 0.003358
-Calc. Vo
0.15
9.
0.4
0.28
0.247526 0.001055
0.036664
10
0.1
11
Km
0.1
12
Vmax
0.309407
0.05
13
14
0.1
0.2
0.3
0.4
0.5
16
17
18
19
Fig. 9. Michaelis-Menten Plot using a value of 0.1 mM for Km.

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Similar questions

Incorrect amino acid changes: Justin (CGC--> AGC) Patient A (GGA-->GAA) Patient B (CGG-->CCG) Patient C (CCT-->TCT) What amino acid changes are associated with the enzymes from the other three patients and how would changes lead to non-functional enzymes?
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
In a plot of 1/v vs 1/[S] for an enzyme-catalyzed reaction, presence of a non-competitive inhibitor will alter the: * Intercept on the 1/v axis. Intercept on the 1/[S] axis. Curvature of the plot. Km
5.50 1/V, min/umol 5.00 4.50 4.00 y = 0.9474x + 2.6649 y = 0.9997x + 2.032 0.00 1.00 2.00 2.50 3.00 1/[S], uM -1 Looking at the double reciprocal plot for an enzyme in the absence of inhibitor and in the presence of two concentrations of inhibitor, what would be the Vmax for the uninhibited enzyme? (bottom graph) Equation is given. Choose the one best answer. 3.50 3.00 2.50 2.00
Calculate KI' of the inhibitor from the information given. All information may not be needed to calculate. K'm = (29Ki+1.45x10^-10)/Ki Vmax = 11.7 µMs-1 Kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM Inhibitor Concentration = 5x10^-12
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
What is the need of adding DNS solution to the enzyme substrate solution? What is the problem in determining rates at low substrate concentration?
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm + a' [S] where Vo is initial velocity, Vmax is maximum velocity, [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches/Vm Vmax 2α' Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. = Apparent, or observed, Km is equivalent to the [S] at which Vo max. apparent Km =
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."
When we compare the binding of I and of S to the enzyme in a mixed noncompetitive inhibitor, we assumed that the binding of I decreased the affinity of the enzyme for S. What would happen if the opposite were true?
Please explain how it is that you approach a problem like this. For example, how would i be able to answer it if instead of met it said Lys, but also explain how you chose the enzyme for met. Thank you, i'll give a positive rate if the taks above is done.
I have a fill in the blank question. "1) Heterophobic or Homotrophic effects= are changes in affinity due to substrate binding and cooperativity between different subunits. They give Allosteric rate curves their Sigmoid shape. 2) Hetero or Homotrophic effects=are changes in affinity due to binding of an effector to an Allosteric site. Allosteric sites are usually 3)located outside or inside the active site. Positive Allosteric effectors (activators) shift the rate curve 4) Left or Right, where Negative effectors shift it 5) right or left. Positive Allosteric effectors usually stabalize the 6)T or R state. Negative efftors usually satbalize the R state." Thank You!!!