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…

Answered: The Michaelis-Menten equation models…

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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Similar questions

At what substrate concentration would an enzyme with a kcat of 33.0 s-1 and a Km of 0.0046 M operate at one-tenth of its maximum rate? Assume the enzyme obeys Michaeli s-Menten kinetics.
An enzyme with an unknown reaction mechanism has been isolated and is being investigated in the lab. Based on the information given below, propose one or more specific catalytic strategies (covalent, acid-base, and/or metal ion catalysis) used by the enzyme and predict the role of each catalytic residue in the enzyme's reaction cycle. Explain your reasoning. (a) Mapping of the active site with substrate analog showed that it contains a critical Ser residue. (b) Studies conducted in buffers of varying pH showed that the enzyme is sensitive to pH changes and has two catalytically important residues with pKa values of ~10.5 and ~4.0. (c) Substitution of the Ser residue with Ala resulted in a five-fold increase in the KM but had no effect on the kcat. (d) The reaction rate was insensitive to the addition of metal chelators such as EDTA and EGTA.
(i) Which graph indicates an enzymatic reaction without inhibitor?(ii) Which type of inhibitor is it? Briefly explain.(iii) Which graph indicates the highest concentration of inhibitor?(iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers.
Quantum tunneling appears to play a significant role in the facilitation of efficient enzyme catalysis in reactions involving the transfer of protons and hydride ions. Provide an energy diagram for a hypothetical reaction in the presence and absence of an enzyme that illustrates the tunneling process.
Can you graph the data
Assume that in a certain cell, the ratio of products/reactants or Keg = 809.5 (Keq is dimensionless) for the reaction Glucose + 2ATP > Glucose-1,6-diP + 2ADP, at a particular instant, the concentrations of each compound were Glucose =2.4M, ATP =11.1M, ADP -12.8M and G-6-P -28.4M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five decimal places
The above graphs (Lineweaver-Burk) were plotted using data from an experiment that investigated changes in initial velocity, V0, (in mmol/min) as a function of substrate concentration, [S], (in mmol/L) for an enzyme-catalysed reaction. The initial velocity was measured at a fixed concentration of enzyme at different concentrations of substrate in the absence of any inhibitor and was then repeated in the presence of a competitive inhibitor at two different concentrations. Use the graph to determine the maximal velocity of the reaction the Km value of the uninhibited reaction the Km value of the reaction with (i) the lower level of inhibitor and (ii) the higher level of the inhibitor. TEMPLATE FOR ANSWERS Vmax of uninhibited reaction Intercept on y-axis = = __________________ Vmax = __________________ Km value of the uninhibited reaction Intercept on x-axis = =…
The above reaction coordinate diagram in the presence of enzyme is inconsistent with the "lock and key" model of enzyme-substrate l binding. Draw and properly label the reaction. coordinate diagram for the enzymatic reaction according to the "lock and key" model. Explain why this model is inconsistent with catalytic properties of enzymes.
For an enzyme-catalyzed reaction, the velocity was determined at two different concentrations of the substrate. Estimate the value of Vmax. [S] (MM) 10 20 88 nmol/min 79 nmol/min 67 nmol/min V(nmol/min) 51 nmol/min 27 Not enough information is given to form a reasonable estimation. 48
Two enzyme catalyzed reactions, RA (red) and Rp (blue), have kinetic profiles shown below. Report which reaction has the higher maximal rate and which reaction has the smaller Km. в A 1/ [S] Higher Vm [ Select ] Lower Km [ Select ] A/T
Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high substrate?

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