What type of inhibition is observed from the shift of the Lineweaver-Burke plot ahown inthe graph below where the solid Ine represents the uninhibited enzymatic reaction while thebroken line represents the inhibited enzymatic reaction?A. Irreveraible inhíbítionB. Noncompetitive inhíbitionC. Competitive inhíbitionD. Uncompetitive inhibitionPotassium cyanide ia a polson which combines with cytochrome A3 to prevent bindingof oxygen to the enzyme without altering the Km of the reaction with respect to reducedcytochrome c. Which type of inhibition does this represent?A. Irreveraible inhibitionc. Competitive inhibitionD. Uncompetitive inhibitionB. Noncompetitiveinhibition_10.Which of the following enzyme classes catalyze reactions in which two molecules becomedissociated from each other?A. Kinaseв. Нуdrolasec. IsomeraseD. LigaseWhich of the following enzyme classes catalyze reactions in which two molecules becomecovalently linked to each other?A. KinaseB. Hydrolase1.C. IsomeraseD. Ligase

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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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Where does inhibitor binds on enzyme in mixed inhibition? A Allosteric site B Binds on substrate C At active site D Does not bind on enzyme
The substrate has been represented bound to the enzyme pocket. 20 Zn Part A: Part B: Substrate Part C: lle Val A Increasing V Arg 1451 (1)=0 Carboxypeptidase A A. Competitive inhibitor B. Irreversible inhibitor C. Allosteric inhibition D. Uncompetitive inhibition E. Non-competitive inhibitor F. -1/KM Benzylsuccinic acid Propose the types of biochemical interactions by which benzylsuccinic acid interacts with the carboxypeptidase A active site. 1. Hydrogen bond II. Ionic bond III.Hydrophobic interactions (Choose from options G-L) Which of the shown Lineweaver-Burk plots would you expect observe when benzylsuccinic acid I used to inhibit Carboxypeptidase A enzymatic activity? (Choose from options N-R) Increasing [1] Benzylsuccinic acid (shown below) has been identified as an inhibitor of carboxypeptidase A. Based on your understanding of enzyme- inhibitor interactions, identify a likely mechanism of inhibition by benzylsuccinic acid. (Choose from options A-E) in-o CH3 1/S) O V.(min) 20…
A. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?
To investigate the effects of a newly discovered inhibitor and enzymology list obtained the results showed in the figure below. Which statement best describes the binding of its inhibitor on the enzyme? ~y=0.768r+4.7425 3-0.568x+46576 19 . . . . ● x X The inhibitor binds at the active site. The inhibitor binds away from the active site, but after substrate binding. The inhibitor binds away from the active site before or after substrate binding. The inhibitor binds close to the active site, but after substrate binding. The inhibitor binds close to the active site, but prior to substrate binding. red by a strain
Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply
Use graphs to illustrate enzyme activity as a function of the following: II. a. Substrate Concentration max velocity v max Rate Substrate Concentration b. Enzyme concentration Rate Enzyme Conc. с. рH Optimum Temperature Increasod temp. results in denaturation Rate Temperature d. Temperature Optimum pH Rate Increas ing pH
An enzyme catalyzes the reaction M-N. The enzyme is present at a concentration of 0.0000000022 M, and the Vmax is 0.0000028 Ms1. The Km for substrate is 5.5 µM. Calculate kcat-
On the energy diagram below, which arrows represent the activation energy? ergy sland Bun bann gran M 1 reaction coordinate 2 3 A. Arrow 1 is the activation energy for both the forward and reverse reactions B. Arrow 1 is the activation energy for the forward reaction and arrow 2 is the activation energy for the reverse reaction C. Arrow 1 is the activation energy for the forward reaction and arrow 3 is the activation energy for the reverse reaction D. Arrow 3 is the activation for the forward reaction and arrow 2 is the activation energy for the reverse reaction
What is true about a competitive inhibitor of an enzyme? You can choose more than one a. it binds the active site b. it binds an allosteric site c. it physically blocks the substrate d. it warps the active site e. it can be overcome with large amounts of substrate
In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor. In each batch, the inhibitor was of a different type: a.Batch 1: competitive inhibitor b.Batch 2:uncompetitive inhibitor c.Batch 3:non-competitive inhibitor Assuming that Vmax = 80 mM s', Km = 8 mM, and Kiof all three inhibitors was 10 mM, which of the inhibitors was the most efficient on Vo? Explain your answer.
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…
Graph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.

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