The following kinetic data were collected for prostaglandin endoperoxide synthase, an enzyme involved in pain and inflammation. Using data in the first two columns, use a graphical analysis to determine the Vmax and the Km of the enzyme. Ibuprofen (Advil) is an inhibitor of prostaglandin endoperoxide synthase. By inhibiting this enzyme, ibuprofen helps to reduce pain and fever. Using the data in the first and third columns, determine the type of inhibition that ibuprofen exerts on prostaglandin endoperoxide synthase. In the presence of the inhibitor, determine the Vmax and the Km of the enzyme. [S] mM Product formed Product formed (mmol/min) with 10 mg/mL ibuprofen 16.67 mmol/min) 0.5 23.5 1.0 32.2 25.25 1.5 36.9 30.49 2.5 41.8 37.04

Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.

Based on the Lineweaver-Burke plot attached.  Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor.  Purified enzyme concentration was 5 µM.  The y-intercept of Lines (A) and (B) is 0.9 sec/uM;  the y-intercept of Line (C) is 0.3 sec/uM.  The slope of Line (A) is 1.8 sec;  the slope of Lines (B) and (C) is 0.6 sec.   Calculate the Vmax of the reaction represented by Line (C).  Show all mathematical work, please.

An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are:     a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare

The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.

Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor.  Purified enzyme concentration was 5 µM.  The y-intercept of Lines (A) and (B) is 0.9 sec/uM;  the y-intercept of Line (C) is 0.3 sec/uM.  The slope of Line (A) is 1.8 sec;  the slope of Lines (B) and (C) is 0.6 sec.   Calculate the Km of the reaction represented by Line (B).

You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table.   ?maxVmax(μmol min−1) ?MKM(mM) Wild‑type 100 10 Mutant 1 0.1 Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1k−1 is much larger than ?2,k2, which of the following statements are correct?   The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax.   Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. ?0=V0=

Based on the Lineweaver-Burke plot attached.  Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor.  Purified enzyme concentration was 5 µM.  The y-intercept of Lines (A) and (B) is 0.9 sec/uM;  the y-intercept of Line (C) is 0.3 sec/uM.  The slope of Line (A) is 1.8 sec;  the slope of Lines (B) and (C) is 0.6 sec. QUESTION:  Line (A) represents ____________.   A. an enzyme-catalyzed reaction in the absence of any inhibitor.   B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor.   C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor.   D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.

Tetrodotoxin  identify the species which releases the toxin (if it is man-made then this will be all that is required for this part) identify the step disrupted in the neuromuscular junction pathway Provide any consequences of this disruption.   Does the toxin have any applications in biomedicine as a painkiller, disease treatment or analgesic? Provide your source in APA format for each.  If this is missing no credit will be awarded.

The initial velocities of two different enzyme-catalyzed reactions were measured over a series of substrate concentrations. The following results were obtained: Enyme A: KM = 1.5 mM, Vmax = 10 μM s-1 Enyme B: KM = 5.0 mM, Vmax = 85 µM s-1 (a) Which enzyme binds to its substrate more tightly (assume k.1 >> k₂ in the Michaelis-Menten model)? (b) Calculate the initial velocities of each reaction when the substrate concentration is 2.5 mM. (c) Calculate the Kcat of each enzyme if the total enzyme concentration is 100 nM. (d) Which enzyme is the more efficient catalyst? Explain your answer. The enzyme carbonic anhydrase is strongly inhibited by the drug acetazolamide. A plot of the initial reaction velocity (as a percentage of Vmax) in the absence and presence of the inhibitor is shown below. What type of inhibition is taking place? Explain your reasoning. V (% of Vmax) 100 50 0.2 0.4 No inhibitor Acetazolamide [S] (MM) 0.6 0.8 1