The fractional saturation of an enzyme is 80% at a substrate concentration of 20 mM. In the presence of 5 mM of a competitive inhibitor the fractional saturation at the same substrate concentration is 40%. The Km for this reaction is mM, and the apparent Km is mM. The value of alpha is while the Ki of the inhibitor is mM.

Q: Under the following conditions, fill in the blanks. Then, describe why this inhibitor is the type of…

A: Enzyme inhibition refers to the decrease in enzyme related process which may be enzyme production or…

Q: The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial…

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

Q: Note the Michaelis Menton kinetics results of inhibition by inhibitor A and by B, separately. Normal…

A: According to our guideline we can answer only the first three subports of the first question. So…

Q: You are trying to come up with a drug to inhibit the activity of an enzyme  thought to have a role…

A: In competitive inhibition, an inhibitor molecule interferes with the binding of normal substrate to…

Q: VO (mM/min), Minus Substrate, mM vO (mM/min), Plus Inhibitor Inhibitor 0.5 23.5 16.67 1 32.2 25.25…

A: In order to solve this problem, we need to draw the Lineweaver Burk (LB) plot. The LB plot has…

Q: The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme:

A: The Michaelis–Menten equation is the rate equation for a one-substrate enzyme-catalyzed reaction.…

Q: in the concerted model of enzyme action when the L ratio (T/R) is 10,000 the velocity vs. Substrate…

A: Enzymes are biomolecules that catalyze (increases the rate of the reaction ) biochemical reactions .…

Q: Please note the reaction expression below. Which of the following rate constants describes the…

A: Michaelis-Menten equation provides us with a general explanation of the velocity and gross mechanism…

Q: A C -1/a K 1-a' Wen a'Nmax (a-1) Var 1/v₂ 1/5) Slope - akma (1) a=1+- am 1 (no inhibitor) Increasing…

A: The Lineweaver–Burk plot or the double reciprocal plot is a graphical representation of the…

Q: An enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM s-. Calculate the reaction…

A: Most of the enzymes follow Michalis-Menten enzyme kinetics. In this equation, Vmax is the maximum…

Q: The table presents the rates of reaction at specific substrateconcentrations for an enzyme that…

A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Q: At a substrate concentration that is much greater than the KM for the reaction, which statement is…

A: The velocity of an enzyme catalyzed reaction is given by: V=Vmax×SKM+SWhere,V= velocity of the…

Q: Km V. (V) 15) + V = [S] max a' = 2 a' = 1.5 (7) -15⁰° max a Vmax 1 [S] MM a'=1 [1]

A: Most of the enzymes have certain kinetic properties. whenever a substrate is added to them, the…

Q: The change in the amount of product B in a reaction which is catalyzed by Enzyme A is given in the…

A: Michaelis menten constant, Km= It is the substrate concentration required to produce half maximum…

Q: A hypothetical enzyme that follows Michaelis-Menten kinetics functions has a substrate concentration…

A: For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Q: In a reaction system, the concentrations of Enzyme-Substrate complex [ES], free enzyme [E] and free…

A: For a reversible reaction, the ratio of the product concentration to the reactant concentration at…

Q: 1² L-^ 0.1 + ||| -4-2 |||| 24 [S]-1, (mM-1) 1, The value of Km for the enzyme depicted by curve A is…

A: Km is the Michelle's menton constant which is equal to the substrate concentration at half of the…

Q: How would Km and Vmax values change if competitive and non-competitive inhibitors are present in an…

A: Enzymes are specialized proteins that act as catalysts in biological systems. By decreasing the…

Q: e) Two 20th century scientists, Leonor Michaelis and Maud Leonora Menten, proposed the model known…

A: Enzymes are the catalytic protein, which increases the rate of reaction by converting the substrate…

Q: sing equilibrium argument, why does Km apparently increase, decrease or stay the same in…

A: Inhibition in biochemistry occurs in different enzymes. Inhibition of enzymes means blocking or…

Q: The following question focuses on how the parameters regulating enzyme function might change, and…

A: Michaelis-Menten (MM) plot and Lineweaver Burk (LB) plot are drawn to decipher the kinetic…

Q: The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme:

A: The Michaelis–Menten equation is the rate equation for a one-substrate enzyme-catalyzed reaction.…

Q: what concentration of a competitive inhibitor is required to yield 60% inhibition of an enzyme at a…

A: For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Q: For some Enzyme, the Vmax is 18 micromols/min, Km is 400 microM. If the substrate concentration is…

A: Velocity of the reaction defines the rate of reaction which is catalyzed by the enzyme. It depends…

Q: You are working on an enzyme that obeys standard Michaelis-Menten kinetics. You have determined the…

A:

Q: Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax of the…

A: Vmax : Reaction rate- when the enzyme gets fully occupied by substrate. Vmax- Maximum velocity

Q: Enzyme X has a Km of 2 µM and a kcat of 104 s1. In the presence of an inhibitor, Km increases to 4…

A: Enzymes are protein molecules that speed up the reactions by decreasing the activation energy.…

Q: Most of the enzyme reactions followed the mathematical kinetic plots suggested by the…

A: The enzyme kinetic parameters are studied using Michalis-Menten kinetic equation.