a. [S] <<< Km
If the [S] is far less than Km, doubling the [S] would result in a
similar increase in reaction rate.
b. [S] = Km
Km = The substrate concentration at which the reaction rate is
Vmax/2
At Km, half od the enzymes' active sites are occupied.
c. [S] <<< Km
At elevated [S], all the active sites on the enzyme are
occupied.
d. [S] <<< Km
At elevated [S], doubling the [S] will have the least effect on the
rate
e. [S] >>> Km
At very low [S], very few (<10%) of the active sites are
occupied.
f. [S] >>> Km
At elevated [S], all the active sites on the enzyme are
occupied.
This condition results in the highest reaction rate.
g. [S] <<< Km
At very low [S], very few active sites on the enzyme are
occupied.
i.e. The [ES] complex is much lower than the free [E]
h. [S] <<< Km
At low [S], the rate is directly proportional to [S]
i. [S] = Km
At Km, [EFree] = [ES]
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the...
The Michaelis-Menten equation models the hyperbolic relationship between [S) and the initial reaction rate V, 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, [S] = Km, and [S] >> K. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V where steady state conditions are assumed. (E l refers to the total enzyme concentration and [Erre refers...
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V for an enzyme-catalyzed, single-substrate reaction E+S E S E+P. The model can be more readily understood when comparing three conditions: (S) <<K.. [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V, where steady state conditions are assumed. Etotal) refers to the total enzyme concentration and Etree refers to the concentration...
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate (V0) 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: \"Rate\" refers to initial velocity (V0) where steady state conditions are assumed; [Etotal] refers to the total enzyme concentration, and [Efree] refers to the concentration of free enzyme. categories: [S]<<Km, [S]=Km,...
The Michaelis-Menten equation models the hyperbolic relationship between (S) and the initial reaction rate V, for an enzyme-catalyzed, single-substrate reaction E+ S E S E+P. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and [S] >> K. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vwhere steady state conditions are assumed. [Exotal) refers to the total enzyme concentration and [Etre) refers to the...
please answer a,b and c. 4. Consider when enzyme E binds to Substrate Sassuming Michaelis-Menten kinetics kz[E]. [S] R= [S] + km a) What is the rate when [S] = km? b) What is the maximum rate (which is achieved when [S] >>> km) c) The rate of the reaction vs substrate concentration is given by the graph below. Indicate the VALUE of half of the maximum rate (Romex/2) and ku using the equations you derived in part a and...
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...
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?
For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity v (as a percentage of Vmax) ,observed at each of the following substrate concentrations. (Ex, v = xVmax, where x = an integer, fraction, or decimal number (two decimal places)) a) [S] = 0.1 Km _________ b) [S] = 2 Km _________ c) [S] = 10 Km _________
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...
9. Applying the Michaelis-Menten Equation I An enzyme catalyzes the reaction A = B. The enzyme is present at a con- centration of 2 nm, and the Vmax is 1.2 ums". The Km for substrate A is 10 um. Calculate the initial velocity of the reaction, Vo, when the substrate concentration is (a) 2 um, (b) 10 um, (C) 30 um.