Shown below is Lineweaver-Burk plot for an enzymatic reaction at different substrate concentrationsin the presence and absence of an inhibitor. The enzyme concentrationis identical in both reactions:1/v (sec/mM)4.543.532.521.510.5000.20.4y = 0.997 +3.01x (+1)0.61/[S] (mM-¹)y = 0.09999 + 3.01x0.8(-1)1(c) What is the type of inhibition mechanism?A. competitive inhibitionB. uncompetitive inhibition (substrate-dependent)C. mixed inhibition(a) Does this enzyme obey Michaelis-Menten kinetics? (yes or no) Explain:D. noncompetitive inhibition (substrate-independent)E. allosteric inhibition1.2(b) What are the apparent values of Vmax and KM for each experiment (with and without inhibitor)?d) If the concentration of the inhibitor is 0.1 mM, what is the value of KI and/or K'I (whichever isrelevant)? (e) Draw v versus [S] for this enzyme in the presence and absence of inhibitor on the plot below (youdo not need to be exact and your axes may not be scaled properly, but use thevariables you calculated in part (A) to label relevant values).v (mm/sec)[S] (MM)

Enzymes kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction…

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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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(i) Which graph indicates an enzymatic reaction without inhibitor?(ii) Which type of inhibitor is it? Briefly explain.(iii) Which graph indicates the highest concentration of inhibitor?(iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers.
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Create a ONE page, formal summary, including APA Formatted in-text citations, of the enzyme amalyze and how it is used in the meat processing industry (Address all guiding questions below in your summary). Note, references can be the second page of the assignment. Include the questions in ur answer Which enzyme is used in the industry (if more than one enzyme is included, you can choose one of the enzymes) Describe the molecular structure of the enzyme (how many amino acids; discuss different levels of protein structure-secondary, tertiary, quaternary, key structural components/amino acids in active site) Describe how the enzyme works in the industry and why it is a key component for this industry. What specific reaction(s) are being catalyzed? What types of bonds are being broken?
When reviewing a Michaelis-Menten Saturation Curve, at first the rate of the reaction is relatively constant, but the rate decreases as the substrate is used up and eventually reaches a plateau. Afte reaching this plateau, what would speed up the reaction again? Adding more substrate Adding heat Adding more enzyme Adding cofactors
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
Describe experimental enzyme inhibition and how it leads to a deeper understanding of enzyme mechanisms. Explain mechanism-based enzyme inhibition. Describe enzyme inhibition by a transition-state analog. For fluoroacetate and hypoglcyin A, explain how each of these mechanism-based inhibitors is converted to the actual enzyme inhibitor and how this inhibitor then inhibits the relevant enzyme..
Describe the specific multi-enzyme example discussed in class of how enzyme activity can be altered by changing its substrate to product ratio.
In a uni uni enzyme reaction, what is the substrate concentration relative to Km when anenzyme operates at 0.95 * V. What about 0.99 * V?
Inhibitors are compounds capable of blocking the catalytic process. Outline with the use of graphs and equations in illustrating the different modes of action of enzyme inhibitors.
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 =
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.

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Shown below is Lineweaver-Burk plot for an enzymatic reaction at different substrate concentrations in the presence and absence of an inhibitor. The enzyme concentration is identical in both reactions: