Please answer asap Enzyme X and Enzyme Y both react with the same substrate S. In each reaction with S, 10 µM ofenzyme is used. Which of the following statements is true concerning these enzymes?Vo (mM/s) Enzyme X0.251[S] mMVo (mM/s) Enzyme Y10.0630.3340.1160.4960.1510.5870.189160.6580.190320.6640.190Enzyme Y has higher substrate specificityEnzyme Y has the higher kcat valueEnzymes X and Y have similar KM values for SEnzyme X and Y have the same substrate specificity constant for SThe affinity is much higher for Enzyme Y with S than it is for Enzyme X with S

A substance called an enzyme acts upon a substrate molecule and decreases the activation energy…

Answered: Enzyme X and Enzyme Y both react with…

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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What is the optimum temperature (degrees Celsius) for the enzyme activity? choices: a,b,c,d,e At what temperature when the enzyme was totally denatured? choices: a,b,c,d,e The graph shows that enzymatic activity is directly proportional to temperature from point A to E. choices: Agree or Disagree
Km of LDH with substrate 1 is 60 M and Km with substrate 2 is 45 M. The enzyme has a higher affinity for substrate 2. true or false
The graph shows the reaction coordinate of an enzymatic reaction of substrate to product a) which number correlates with the overall Keq of the reaction going from S to P? b) which number correlates with the velocity of the reaction WITHOUT enzyme (ie. starting with only substrate)? C) which number correlates with the overall velocity of the reaction WITH SATURATED enzyme D) the initial velocity of this reaction increases by a specific factor in the presence of enzyme. The difference between which two numbers best correlates with this enhancement in velocity? 1) 3 and 1 2) 3and 2 3) 3 and 4 4) 3 and 5 5) 3 and 6
Which of the following describe what enzymes such as Chymotrysin accomplish to allow products to form and be released by the enzyme active site? Group of answer choices catalyze chemical eactions that are thermodynamically unfavorable to occur establish a more stable transition state at a higher energy level to perform a catalysis reaction redce the chemical energy held within a chemical bond modify chemical structure of a substrate to "fit" within the active site
What effect is seen on a Lineweaver-Burke graph when a competitive inhibitor is added to an enzymatic reaction? neither the y-intercept nor the slope change both the y-intercept and the slope change the slope of the line changes the line is inversed the y-intercepts changes
A researcher has developed an assay to measure the activity of an important enzyme present in pancreatic cells growing in culture. She adds the enzyme's substrate to a dish of cells and then measures the appearance of reaction products. The results are graphed as the amount of product on the y-axis versus time on the x-axis. The researcher notes four sections of the graph. For a short period of time, no products appear (section A). Then (section B) the reaction rate is quite high (the slope of the line is steep). Next, the reaction gradually slows down (section C). Finally, the graph line becomes flat (section D). Draw and label the graph, and propose a model to explain the molecular events occurring at each stage of this reaction profile.
Which of the following statement about the enzyme thermodynamics is TRUE? a. Enzymes increase the activation barrier (∆G cat) of the products b. Enzymes decrease the activation barrier (∆G cat) of the products c. Enzymes decrease the free energy (∆G) of the products d. Enzymes decrease the free energy (∆G) of the reactants e. Enzymes increase the activation barrier (∆G cat) of the reactants
The enzyme activity is: A. to The number of grams of substrate that react to form product, per mole of enzyme, per unit of time. b. The number of moles of substrate that react to form product, per gram of enzyme, per unit time. c. The number of moles of substrate that react to form product, per mole of enzyme, per unit time d. The number of grams of substrate that react to form product, per gram of enzyme, per unit of time.
The image shows the rate of an enzyme reaction under conditions of no inhibition, competitive inhibition, and noncompetitive inhibition as reactions labeled uninhibited, A, and B. Which of the following best explains what has occurred in the enzyme reactions? Reaction B shows competitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows noncompetitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows competitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor. Reaction B shows noncompetitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor.
When substrate [S] = Km, the velocity of an enzyme catalyzed reaction is about: * 0.1 Vmax. 0.2 Vmax. 0.5 Vmax. 0.9 Vmax
The quantity of enzyme needed to convert 1 µ mole of substrate to products in one minute is called the enzyme a. efficiency b. turnover number c. international unit d. specificity e. no correct response is given
When the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increases

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