The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V for anenzyme-catalyzed, single-substrate reaction E + SES →E + P. The model can be more readily understood whencomparing three conditions: [S] << Km. [S] = Km, and [S] >> Km.Match each statement with the condition that it describes.Note that "rate" refers to initial velocity V, where steady state conditions are assumed. [Etotal] refers to the total enzymeconcentration and [Efree] refers to the concentration of free enzyme.[S] << KmIncreasing [Ewall will increase Km.Almost all active sites are empty.[S] = KmAnswer Bank[Enel is about equal to [Exotal].[ES] is much higher than [Efree][S] >> KmReaction rate is independent of [S].Not true for any of theseconditionsThe rate is half of the maximum rate.

Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate for an enzyme-catalyzed, single-substrate reaction E+SES →E+P. The model can be more readily understood when comparing three conditions: [S] << Km. [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] << Km Increasing [Ex] will increase Km. Almost all active sites are empty. [S] = Km Answer Bank Eael is about equal to Eatal [ES] is much higher than Ene [S] >> Km Reaction rate is independent of [S]. Not true for any of these conditions The rate is half of the maximum rate.

The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate for an enzyme-catalyzed, single-substrate reaction E+SES →E+P. The model can be more readily understood when comparing three conditions: [S] << Km. [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] << Km Increasing [Ex] will increase Km. Almost all active sites are empty. [S] = Km Answer Bank Eael is about equal to Eatal [ES] is much higher than Ene [S] >> Km Reaction rate is independent of [S]. Not true for any of these conditions The rate is half of the maximum rate.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

See similar textbooks

Similar questions

Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
Based on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surely
In the scheme for enzymatic catalysed reaction proposed by Michaelis and Menten, the steps involve reversible formation of enzyme-substrate (ES) complex followed by conversion of the complex to the product (P). a) Derive the rate equation for enzymatic process. State an assumption made in this derivation. Terbitkan persamaan kadar tindak balas bagi proses enzim. b) By showing appropriate reaction mechanisms and rate equations, explain how enzyme catalytic reactions may be affected by competitive inhibition
In 1966, Ferdinand showed that a random-order ternary-complex mechanism for a two-substrate enzyme-catalysed reaction can lead to sigmoidal kinetics being observation in the absence of cooperative binding. Discuss this scenario so that it is clear why a plot of Vo versus [AXo] at constant [Bo] will be sigmoidal.
Compare and contrast Bound Fraction equation in ligand binding and Michaelis-Menten equation in enzyme kinetics, including their double-reciprocal forms. Discuss what Km is important for and what Vmax (or kcat) is important for? Under what (substrate) conditions is Km more important than Vmax, and under what (substrate) conditions is Vmax more important than Km? Based on the discussions in question 2, explain what type of inhibitors works best under (a) high substrate concentration and (b) low substrate concentration.
If a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.
For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s -1 , k-1 = 3.1 ⅹ 104 s -1 , and k2 = 3.4 ⅹ 105 s -1 . a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach rapid equilibrium or the steady state? Show work justify b) What is kcat for this reaction? Show work justify c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1 , and each enzyme has two active sites.
The following reaction sequence consists of two different substrates catalyzed by an enzyme:let's assume he described his reactions.;E + S1: ES1ES1 + S2: ES1S2ES1S2 → P + Ea.Derive the reaction velocity equation with Michaelis-Menten acceptance.b. Derives the rapid equality of S1 substrate concentration, rather than S2 substrate concentrationsimplify for reaction cards where it is higher.
If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.
Consider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence ofinhibitor I: Using a Michaelis-Menten plot, determine Km for theuninhibited reaction and the inhibited reaction.
Calculate the standard free-energy change of the reaction catalyzed by theenzyme phosphoglucomutase, given that, starting with 20 mM glucose 1-phosphate and no glucose 6- phosphate, the final equilibrium mixture at 25 °C and pH 7.0 contains 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. Does the reaction in the direction of glucose 6-phosphate formation proceed with a loss or a gain of free energy?
1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the inhibitor icreaces, what can be said about the mode of inhibition and why? 1.3) calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this? 1.4) discuss the mechanism of the bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues. make use of relavant graphs and diagrams to explain your answer.