BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 8, Problem 35P
Interpretation Introduction
Interpretation:
The effect of the mutation on the catalytic rate of an enzyme if the binding of the transition state is unaffected is to be stated.
Concept introduction:
The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
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At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
Some enzymes have catalytic activity only limited by diffusion. Which rate constants of an enzyme- catalyzed reaction is/are rate limiting for the enzyme? How does this line up/compare to the rate limiting step of Michaelis-Menten Enzyme Kinetics?
(Please show work and correct answer)
The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km.
Match each statement with the condition that it describes.
Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.
Chapter 8 Solutions
BIOCHEMISTRY-ACHIEVE (1 TERM)
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
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- When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.arrow_forwardThe Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an enzyme-catalyzed, single-substrate reaction E + S ES → E + P. The model can be more readily understood when comparing three conditions: [S] > Km- Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Not true for any of these conditions Almost all active sites will [ES] is much lower than [Efree]. be filled. The rate is directly proportional to Increasing [Etotal] will increase [S]. Km: Adding more S will not increase [Efree] is equal to [ES]. the rate.arrow_forwardIn enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.arrow_forward
- When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C 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 substratesarrow_forwardIn enzyme kinetics, for the reversible with one complex mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicates forward direction while the variables denoted with b indicate backward direction.arrow_forwardWhich of these statements about enzyme-catalyzed reactions is false? The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction. The Michaelis-Menten constant Km equals the [S] at which V = 1/2 V, max: At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. The rate of a reaction decreases steadily with time as substrate is depleted. If enough substrate is added, the normal V, of max a reaction can be attained even in the presence of a competitive inhibitor.arrow_forward
- The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the micro environment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.arrow_forwardAn example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism is the hydrolysis of peptides by chymotrypsin while, Lysozyme is often cited as an example of an enzyme which operates by strain mechanism. Discuss both mechanisms in the context of each enzyme.arrow_forwardSuppose that a mutant enzyme binds a substrate 100 times as tightly as does the native enzyme. What is the effect of this mutation on catalytic rate if the binding of the transition state is unaffected?arrow_forward
- Explain why the very tight binding of a substrate to an enzyme is not desirable for enzyme catalysis, whereas tight binding of the transition state is desirable.arrow_forwardAn uncatalyzed reaction has keq=50. in the presence of an appropriate enzyme.the forward rate of the reaction increased by 20-fold.what is the equilibrium constant in the presence of the enzyme?arrow_forwardwhen saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.arrow_forward
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