Answer Happy

The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an enzyme-catalyzed, single-substrate reaction E+SESE + P. The model can be more readily understood when comparing three conditions: [S] << Km. [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Eotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] << Km [ES] is much lower than [E]. [Etree] is about equal to [E]. incorrect [S] = Km This condition rarely occurs for most in vivo enzymes. [Efree) is equal to [ES]. Answer Bank [S] >> Km Almost all active sites will be filled. Not true for any of these conditions Increasing [Eall will lower Km.
A plot of V, on the y-axis versus Vo/ [S] on the z-axis is known as an Eadie-Hofstee plot. Like the Lineweaver-Burk plot, the Eadie-Hofstee plot is derived from a transformation of the Michaelis-Menten equation. The Michaelis-Menten equation expresses the relationship between the following terms: Vo, the rate of reaction; Vmax the maximal rate; . [S], the substrate concentration; and KM, the Michaelis constant. Rearrange the Michaelis-Menten equation to obtain the Eadie-Hofstee equation, giving Vo as a function of Vo/[S]. Vo -KM TS+Vmax- In an Eadie-Hofstee plot, what is the significance of the x-intercept? 1/[S] -KM Vmax Vmax/KM
The Eadie-Hofstee plot illustrated shows enzyme activity in the absence of an inhibitor. Adjust one or both points so that the line shows enzyme activity in the presence of a competitive inhibitor. 20 NGISTR558 19 18 17 Incorrect 16 15 13 12 11 10 9 8 7 6 5 4 3 2 1 0 0 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 V./[S]