Q4: Got it wrong. I recieved feedback on it. The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for anenzyme-catalyzed, single-substrate reaction E + SES →→ E + P. The model can be more readily understood whencomparing 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. [Etotal] refers to the total enzymeconcentration and [Efree] refers to the concentration of free enzyme.[S] << Km[ES] is much lower than [Efree].Increasing [Etotal] will lower Km.Incorrect[S] = KmHalf of the active sites are filledwith S.[S] >> Km[Efree] is about equal to [Etotal].Almost all active sites willbe filled.Answer BankNot true for any of theseconditionsThis condition rarely occurs formost in vivo enzymes.< FeedbackMacmillan LearningXAt least one statement is not matchedto its correct condition. At low Sconcentration, most of the enzyme is inthe [Efree] form.

Those proteins or biological catalysts which help to speed up the chemical reaction are termed…

-catalyzed, single-substrate reaction + S ring three conditions: [S] << Km, [S] = Km, and [S] >> Km. each statement with the condition that it describes. at "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme tration and [Efree] refers to the concentration of free enzyme. [S] << Km ES] is much lower than [Efree]. creasing [Etotal] will lower Km- [S] = Km Half of the active sites are filled with S. model can be more readily understood when [S] >> Km [Efree] is about equal to [Esotal]. Answer Bank Almost all active sites will be filled. Not true for any of these conditions This condition rarely occurs for most in vivo enzymes. Ⓒ Macmillan Learning At least one statement i to its correct condition. concentration, most of t the [Efree] form.

-catalyzed, single-substrate reaction + S ring three conditions: [S] << Km, [S] = Km, and [S] >> Km. each statement with the condition that it describes. at "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme tration and [Efree] refers to the concentration of free enzyme. [S] << Km ES] is much lower than [Efree]. creasing [Etotal] will lower Km- [S] = Km Half of the active sites are filled with S. model can be more readily understood when [S] >> Km [Efree] is about equal to [Esotal]. Answer Bank Almost all active sites will be filled. Not true for any of these conditions This condition rarely occurs for most in vivo enzymes. Ⓒ Macmillan Learning At least one statement i to its correct condition. concentration, most of t the [Efree] form.

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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