The Michaelis Menten Equation Models The Hyperbolic Relationship Between S And The Initial Reaction Rate Vo For An Enz 1 (92.04 KiB) Viewed 10 times
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate Vo 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 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.
An enzyme catalyzes a reaction with a Km of 7.00 mM and a Vmax of 1.50 mM s¹. Calculate the reaction velocity, vo, for each substrate concentration. Vo Vo : [S] = 2.25 mM [S] = 7.00 mM mm. s-1 mM. s-1
Vo : [S] = 14.0 mM mM. s-1
One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Ribonuclease Fumarase Lactate dehydrogenase Urease fumarate molecules: How many molecules of fumarate can one molecule of fumarase act on in 13.4 min? 9000000 Substrate Turnover number (per second) RNA fumarate lactate urea Incorrect 100 800 1000 10,000
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