Consider this intermediate in the derivation of the Michaelis-Menten equation.[E] [S][ES|k-1 + kzkmAssume that k is negligible compared to the other rate constants.If the k is very small, it suggests that the enzyme has a Select an optionaffinity for its substrate, while if the if the km is very large, itsuggests that the enzyme has a Select an option.affinity for its substrate.Select an optionSubmitYou have used 0 of highSavlowmoderate

Km : The concentration of substrate at which enzyme achieves half Vmax-maximum velocity

Answered: Consider this intermediate in the…

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

Draw a hypothetical Michaelis-Menten plot for an enzyme reaction (i) without and (ii) with a pure noncompetitive inhibitor. Label Vax and Km on plot
Please answer A & B attached with image.
Given the following reaction and equation for the initial velocity of the reaction: k₁ k3 E+S ES E + P V=Keat [ES] = k3 [ES] k₂ where keat is the rate constant for the reaction which forms the product from the ES complex. Explain in words why the velocity is directly proportional to theamount of enzyme added in the presence of saturating substrate levels.
Consider an enzyme that catalyzes the reaction S2 P, by the following simple reaction mechanism: k, E + S 2 E•S →E kcat + P Suppose the enzyme acquires a mutation that causes k1 to be 10-times smaller than for the wild-type (non-mutant) enzyme. Suppose you measure the initial reaction rate (vo) at several different [S] for the mutant and the wild-type enzymes. Under what conditions would the mutation have a greater effect on the reaction rate (vo) of the mutant enzyme compared to the wild-type enzyme - at very low [S], or at very high [S]? Explain briefly how you decided.
In the scheme below which represents the mechanism of action for a large number of enzymes: A+B⟺AB⟶C The steady state approximation is reached when: d[AB]/dt≈0 k2≫k1 k−1≫k1 k−1=k1
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
Many enzyme -catalyzed reactions are consistent with a modified version of the Michaelis -Menten mechanism in which the second step is also reversible. For this mechanism obtain an expression for the rate of formation of product and find its limiting behavior for large and small concentrations of substrate using steady state approximation
The reaction: A + B <-> P + Q is catalysed by enzyme E. Draw a Cleland diagram for a Non-sequential (Ping-Pong) mechanism for this reaction.
Solve the Michaelis-Menten equation for KM when vo=Vmax/2. What does this tell you about the relationship between substrate concentration and enzymes with high KM values? With low KM values?
(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.
When enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.
Derive the rate law for the following enzyme reaction chain. Linear the equation you have derived as a Lineweaver-Burk type equation.

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