Match each statement with the condition that it describes. Note that "rate" refers to initial velocity $V_0$ where steady state conditions are assumed. $[E_{total}]$ refers to the total enzyme concentration and $[E_{free}]$ refers to the concentration of free enzyme. $[S] << K_m$ $[S] = K_m$ $[S] >> K_m$ Not true for any of these conditions Answer Bank Almost all active sites will be filled. Half of the active sites are filled with S. $[ES]$ is much lower than $[E_{free}]$. This condition rarely occurs for most in vivo enzymes. The rate is directly proportional to $[S]$. Increasing $[E_{total}]$ will lower $K_m$.
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This means that the enzyme is not saturated with substrate, and the rate of the reaction is directly proportional to the concentration of substrate. Show more…
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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, [S] = Kₘ, and [S] >> Kₘ. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V₀ where steady state conditions are assumed. [Eᐓₒᐓₐₗ] refers to the total enzyme concentration and [Eₒᐅₑₑ] refers to the concentration of free enzyme. [S] << Kₘ [S] = Kₘ [S] >> Kₘ Not true for any of these conditions Almost all active sites are empty. The rate is directly proportional to [S]. Half of the active sites are filled with S. [ES] is much higher than [Eₒᐅₑₑ]. This condition rarely occurs for most in vivo enzymes. Increasing [Eᐓₒᐓₐₗ] will lower Kₘ. Answer Bank
Shaiju T.
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, [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "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. [S] << Km [S] = Km [S] >> Km Not true for any of these conditions Almost all active sites are empty. The rate is half of the maximum rate. [ES] is much higher than [Efree]. Increasing [Etotal] will lower Km. Answer Bank [Efree] is about equal to [Etotal]. Reaction rate is independent of [S].
Madhur L.
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, [S] = Km, and [S] >> Km. Match each statement with the condition that it describes. Note that "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. [S] << Km [S] = Km [S] >> Km Not true for any of these conditions The rate is directly proportional to [S]. Almost all active sites are empty. Half of the active sites are filled with S. This condition rarely occurs for most in vivo enzymes. Increasing [Etotal] will increase Km. [ES] is much higher than [Efree]. Answer Bank
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