Derive the equation
Vm.t = So-S + Km.ln(So/S)
from Michaelis - Mantens equation
(Vo=Vm.S/(Km+S))
(Bio Chemical Question)
Derive the equation Vm.t = So-S + Km.ln(So/S) from Michaelis - Mantens equation (Vo=Vm.S/(Km+S)) (Bio Chemical...
Derive the Michaelis -Mantens equation for enzymatic reaction ? What will happen if there are no enzyme in this process. Bio chemical question
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?
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?
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...
(5) The Michaelis-Menten equation describes the following simplistic pathway Km (a) State each of the assumptions on which the Michaelis-Menten equation is based. (b) Derive the rate law for this process
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...
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
Kcat =30.0 s-1 Km= 0.005 M Operating at 1/4 Vmax What is [S] ? The solutions manuel doesn't explain the problem well. Whete does the 0.33 km come from? For part 2 : Plug in [S]= 1/2 Km, 2 Km, and 10 Km Where does the 1.5 Km come from? Answer (a) Here we want to find the value of [S] when Vo = 0.25 V max. The Michaelis-Menten equation is V = Vmax[S]/(Km + [SD so V = Vmax...
Derive the Michaelis-Menten equation. Convert the derived equation to a linear form.
derive michaelis menten equation please show steps