One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover
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One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover
The protein catalase catalyzes the reaction 2 H,O,(aq) 2 H₂O(l) + O₂(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 x 107 s-¹. The total enzyme concentration is 0.017 µM and the initial substrate concentration is 6.10 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax = R = 1360 Incorrect Calculate the initial rate, R (often written as Vo), of this reaction. 0.3317 Incorrect mM-s-1 mM-s-1
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo for an enzyme-catalyzed, single-substrate reaction E+ SES → 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 Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] << Km [ES] is much lower than [Efree]. [Efree] is about equal to [Etotal]. Incorrect [S] = Km This condition rarely occurs for most in vivo enzymes. [Efree] is equal to [ES]. [S] >> Km Almost all active sites will be filled. Answer Bank Not true for any of these conditions Increasing [Etotal] will lower Km.