2. Indicate whether each of the following statements describes a reversible competitive inhibitor,reversible noncompetitive inhibition, or an irreversible inhibitor.a. It bonds covalently to the active siteb. The inhibitor effect can be reversed by the addition of more substratec. Inhibitor structure resembles that of the substrated. The inhibitor and substrate cannot bind to the enzyme simultaneously.

Enzymes are usually protein molecules which catalyzes the biochemical reaction by decreasing its…

Answered: 2. Indicate whether each of the…

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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Draw the graphs representing activity behavior for each uncompetitive Inhibition, non-competitive Inhibition, and competitive Inhibition. Please use a ruler, draw, photograph, and insert the image in this document. Label x and y axes, Km and Vmax.
A plot of 1½5 venut VSL, Glld a Br-weaver Burk or double-reciprocal plot, is a useful tool for identifying the type of Madily each gaph by dragging the endpoints to show the various types of enzyme inhibition. What is the inhibition mechanism for the competitive inhibitor? The inhibisr binde cenly in recemyne The inhibitor bindx only lo cozyme- substrate complexe The inhibike binds tas bath free enzyme and enzyme xubxirale completes with identical binding axolante. The inhibikr binds to both free enzyme and cozyme substrate completes with different binding constants. What is the inhibition mechaniam for the uncompetitive inhibitor? The inhibitor binds only to free ENZYMES. The inhibitor bind is both tree enzyme and enzyme auhdraic compleaca with identical binding coulants. The inhibar binds only in enzyme ubrale complex.ca. The inhibir bindis in bath free enzyme and cxyme aubairale complicaca with dill crcnt binding costanix. LAST Nompumps dve shk with inbibus WHEY Pullie mechanism kot…
What is the differences between competitive, noncompetitive, mixed noncompetitive and uncompetitive inhibition in terms of their respective modes of inhibition??
4. Compare and contrast the mechanism used by competitive and noncompetitive enzyme inhibitors. Which type of inhibitor can be "out-competed" by adding extra substrate to a reaction?
Distinguish between Competitive and non-competitive inhibition.
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
3. Enzyme specificity. To determine the specificity of substrate binding for a particular enzyme/protein, structurally related compounds may be used as potential substrates and Km values may be calculated. However, many compounds structurally related to the substrate may bind to the active site but cannot be converted to product. In these instances, the substrate analogs are used as potential competitive inhibitors of substrate binding. Low K, values indicate high affinity of the enzyme for the inhibitor, whereas high K,values indicate low binding affinity. Consider the enzyme xanthine oxidase, which catalyzes the formation of uric acid from the purine bases hypoxanthine or xanthine in humans. The Km for hypoxanthine is 15.0 μM and for xanthine it is 45.0 μM. A few compounds used as competitive inhibitors of the normal substrate hypoxanthine are listed in the table below with their K; values. Comparing the structures of hypoxanthine with the listed substrate analogs, what can you…
1. ( . tion can be represented by the so-called Michaelis equation ) The velocity of an enzyme catalyzed reac- Vmax [S] Vo = Km Vo = max kcat [Eo] [So] (Км + [Sol) V max where [So] is the initial substrate concentration, [Eo] is the total enzyme concentration, kcat is the cataly- tic rate constant or turnover number, and KM repre- sents the Michaelis constant. The graph on the right illustrates the dependence of the velocity of the reaction as a function of substrate concentration. Ex- Km [S] (mm) plain why the maximal velocity can be represented by the expression Vmax = Kcat [Eo] at very high substrate concentrations. Vo (µm/min)
1. Describe the two ways by which the activity of an enzyme can be inhibited.
There is an enzyme inhibition mechanism that is not too detrimental when viewed from the size of Km, namely the inhibition mechanism.... A. non-competitiveB. non-competitive and uncompetitiveC. in-competitive and uncompetitiveD. in-competitiveE. uncompetitive
1. Which of the following statements is/are TRUE for both the concerted and sequential models of allosteric enzymes? a. follows the induced-fit model b. the activator can only bind to the R form c. the inhibitor can only bind to the T form d. the substrate can only bind to the R form 2. Which of the following describes the efficiency of enzymatic catalysis? a. [S] b. KM c. Vmax d. kcat
14. In competitive inhibition, an inhibitor— binds reversibly at the active site. binds to both free enzyme and the ES complex. binds at several different sites on an enzyme. binds only to the ES complex. binds covalently to the enzyme.

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2. Indicate whether each of the following statements describes a reversible competitive inhibito reversible noncompetitive inhibition, or an irreversible inhibitor.