1)Derivation of the Michaelis -Menten equation. I want you to show every single step
The equation that describes the above Michaelis-Menten curve: Vo TS]+K Vmax [S] Michaelis-Menten Equation Lineweaver and Burke manipulated the Michaelis-Menten equation to yield: Ko V I S Vmax [S] Lineweaver-Burke Equation Linewenver Burke Equation If you plot 1/ V. vs. 1/[S], you get the following Lineweaver-Burke plot: 1/V. Slope = km/Vmax Intercept = -1/KM -Intercept = 1/Vmax 1/[S] Which is easier to calculate values for Km and Vmax, using the linear (y=mx+b) Lineweaver-Burke Plot or the Michaelis-Menten curve?
derive michaelis menten equation please show steps
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
1. (15 points) Give the Michaelis-Menten equation and define each term in it (no need to derive the equation). Does this equation apply to all enzymes? If not, to which kind does it not apply?
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...
12)Show work step by step 13)Show work step by step Below is BoX 6-1 if needed Applying the Michaelis-Menten Equation IV An enzyme is found that catalyzes the reaction X= Y Researchers find that the Kyn for the substrate A is 4 pm, and the keat is 20 min . (a) In an experiment, (X) = 6 mm, and the initial velocity, V, was 480 nm min!. What was the (E) used in the experiment? (b) In another experiment, (E)...
1. Note the similarity between the Michaelis-Menten equation [S] = V max [S] + KM pO2 and the oxygen dissociation equation for myoglobin Explain the relationship between the two equations. Y= pO2 + P 50
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...