A high KM will result in an efficient enzyme.A. TrueB. FalseSpecificity constant = Kcat/ KMkcat=Vmax[ET]A high Vmax will result in an efficient enzyme.A. TrueB. FalseTotal enzyme concentration will have no effect on the efficiency of anenzyme catalysed reaction.A. TrueB. False

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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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D. Question 14 Consider the Lineweaver-Burk plots of two enzyme activities on the left. How is enzyme A different from enzyme B? 1/v B 1/[S] O Enzyme A has a negative Km O Enzyme A requires more substrate to achieve the same rate O Enzyme A has a smaller Km/Vm ratio Enzvme A is slower
You are performing an enzyme kinetics experiment testing the effect of pH on reaction rate. You accidentally one of the tubes to react two minutes longer than the other samples. How would this affect the interpretation of the data you obtain for that one tube? A. No change in the interpretation of your data OB. Your data would represent an underestimate of the enzyme's activity at that one pH. OC. Your data would represent an overestimate of your enzyme's activity at that one pH. D. All of the data would be invalid.
In competitive inhibition, increasing concentrations of the inhibitor will have the following effect on the kinetics of the enzyme: A. Km will decrease. B. Vmax will stay the same. C. The reaction will cease because the inhibitor binds irreversibly. D. Km / Vmax will stay the same.
A mixed inhibitor (sometimes called a mixed non-competitive inhibitor) of an enzyme: a decreases both Km and V-max. b increases Km and decreases V-max. c increases Km without altering V-max. d decreases Km without altering V-max.
Which statements are true of an inhibitor that binds the active site of an enzyme? Select all that apply, there may be one correct answer or several. a These inhibitors are a kind of allosteric regulator that decreases enzyme activity. b Adding more substrate can reduce the effect of these inhibitors. c These inhibitors compete with the substrate for the active site of the enzyme. d These inhibitors increase the rate of enzyme activity. e These inhibitors function by changing the shape of the enzyme, stopping if from binding to substrate.
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.
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
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
Identify the conditions that may affect enzyme activity in a reaction. SELECT ALL THAT APPLY A. Increasing Temperature B. Decreasing Substrate C. Lack of coenzyme D. Decreasing pH
When measuring reaction velocity as a function of substrate concentration, a researcher usually keeps the concentration of enzyme at a constant level. What would happen if the enzyme concentration were not kept constant? A. Vmax would change, but Km would remain constant. B. Both Vmax and Km would change C. Vmax would remain constant, but Km would change D. Vmax would remain constant, but V would change E. None of the above would necessarily occur
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.
In drug development, enzyme inhibition studies play a very important role since drugs are often used to target specific enzymes, as illustrated in the example of lovastatin. An important consideration when assessing drug potential is the drug's affinity for the selected target. (The higher the affinity, the better the candidate.) The K₁ is often used in studies to measure the affinity of drug candidates toward their target. Based on your understanding of K₁, which drug would be the BEST candidate for further development? Drug C: K₁= 9.1 x 107 M Drug E: K₁ = 3.5 × 10³ mm Drug D: K₁=5.5 × 10³ μM Drug B: K₁=2.5 × 10 mm Drug A: K₁=4.5 x 10 mm

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A high KM will result in an efficient enzyme. A. True B. False Specificity constant = Kcat/ KM kcat = Vmax [ET] A high Vmax will result in an efficient enzyme. A. True B. False Total enzyme concentration will have no effect on the efficiency of an enzyme catalysed reaction. A. True B. False