Which of the following statements is true about effect of substrate concentration on enzymeactivity ?The rate of reaction increases as the substrate concentration increases up to certainlimit at which the reaction rate is maximal (Vmax.)At Vmax, the enzyme is completely saturated with the substrate,At Vmax, any increase in substrate concentration don't affect the reaction rate.All of them

The formation of an enzyme-substrate complex is the first step in enzymatic catalysis. The enzyme…

Answered: Which of the following statements is…

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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assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?
please make sure the answer you provide is correct i submitted this question differnt times and everytime i got a differnt answer
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
the Km of an enzyme for its substrate is 50mM. At what concentration of substrate would the enzymaticslly catalyzed reaction be at 60% maximum - 30 - 60 -75 - 50 -80
can you explain using a drawing presenting the factors like pH, temperature, substrate concentration, and enzyme concentration on its effect on the activity of an enzyme. You may use graphs or images to explain your ideas. Thank you!
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
1. ( . tion can be represented by the so-called Michaelis equation ) The velocity of an enzyme catalyzed reac- Vmax [S] Vo = Km Vo = max kcat [Eo] [So] (Км + [Sol) V max where [So] is the initial substrate concentration, [Eo] is the total enzyme concentration, kcat is the cataly- tic rate constant or turnover number, and KM repre- sents the Michaelis constant. The graph on the right illustrates the dependence of the velocity of the reaction as a function of substrate concentration. Ex- Km [S] (mm) plain why the maximal velocity can be represented by the expression Vmax = Kcat [Eo] at very high substrate concentrations. Vo (µm/min)
With a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the above
Please help with both the parts
When k2 >> k-1, KM approximates the affinity of the enzyme•substrate complex.The (circle one) higher / lower the KM, the more tightly the enzyme binds to its substrate
The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?
Which statement is NOT completely true? O In the Induced-fit theory, the conformation of the active site changes to accommodate an incoming substrate. O A urease which hydrolyzes only urea is an example of an enzyme that exhibits relative specificity. O Cofactors that are organic also go by the name coenzymes O Many enzymes require a second substance present (cofactor) in order to be active. O Enzymes are protein based catalysts. O Enzymes are sensitive to heat and pH O Enzymes catalyze at their "active site". O Apoenzymes are inactive enzymes.

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