According to the Michaelis-Menton kinetics theory, when a reaction is performed in zero-order kinetics:Please select the single best answer The substrate concentration is very low and the reaction rate is dependent on the substrate concentration The substrate concentration is in excess and the reaction rate is dependent on the enzyme concentration The enzyme concentration is in excess and the reaction rate is dependent on the substrate concentration The substrate concentration is equal to Km and the reaction rate is dependent on the enzyme concentration
Question
According to the Michaelis-Menton kinetics theory, when a reaction is performed in zero-order kinetics:Please select the single best answer The substrate concentration is very low and the reaction rate is dependent on the substrate concentration The substrate concentration is in excess and the reaction rate is dependent on the enzyme concentration The enzyme concentration is in excess and the reaction rate is dependent on the substrate concentration The substrate concentration is equal to Km and the reaction rate is dependent on the enzyme concentration
Solution
The correct answer is: The substrate concentration is in excess and the reaction rate is dependent on the enzyme concentration.
In zero-order kinetics, the rate of the reaction is independent of the concentration of the substrate. This usually occurs when the substrate concentration is so high that all the enzyme active sites are occupied, making the reaction rate dependent on the enzyme concentration.
Similar Questions
Which of the following statements is/are correct in enzyme kinetics, if S represents the substrate?Group of answer choicesAt very low substrate concentration, the rate of enzyme reaction is zero order with respect to [S].At all substrate concentrations, the rate of enzyme reaction is first order with respect to [S].At very high substrate concentration, the rate of enzyme reaction is first order with respect to [S].At very high substrate concentration, the rate of enzyme reaction is zero order with respect to [S].At all substrate concentrations, the rate of enzyme reaction is zero order with respect to [S].
Which of the following best describes the assumption made in steady state kinetic analysis?Group of answer choicesThe concentration of the substrate is decreasing.The concentration of the substrate is constant.The formation of the enzyme-substrate complex is the rate-limiting step.The concentration of enzyme-substrate complex is constant.The enzyme-substrate complex is quickly transformed into the product and free enzyme.
In which order the rate of reaction does not depend on the concentration of reactant
Use the Michaelis-Menten equation to complete the enzyme kinetic data set shown below (fill in the blanks), when Vmax is known to have a value of 100 nM/min. Answer with three significant digits.Substrate concentration (µM) Reaction rate (nM/min)4.00 50.05.00 10.0 20.0
All of the following are true of enzyme-catalyzed reactions EXCEPT:A.the presence or absence of a post-translational modification may alter the activation energy Ea of the reaction.B.the enzyme does not affect the net reaction rate if the ratio of products to reactants equals Keq for the reaction.C.substrates can covalently modify the enzyme to cause a permanent decrease in the enzyme's turnover number kcat.D.the saturation of enzyme active sites by substrate molecules limits the maximum reaction velocity Vmax.Submit
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