Which of the following is the most efficient enzyme An enzyme with a high kcat and a high Km. An enzyme with a low kcat and a low Km. An enzyme with a high kcat and a high Km. An enzyme with a high kcat and a low Km.
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- The order of the data in the table is reversed. Pay attention and calculate straight. Some experiments have been done using a fixed amount of enzyme. Made in different substrate concentrations. The table below contains data. S( mM/L-min) V( mM/L-min) 2000 155 1000 150 200 120 100 100 60 80 40 64 20 40 10 20 Find Vmax and Km using all data points and at least two linear transformationsan enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form CAn enzyme facilitate catalysis by formation of ester bond with an alcoholic substrate. Which amino acid residues can facilitate such mechanism of catalysis? Select the correct response: Cys and Met Lys and Arg Ser and Tyr Glu and Asp
- Which of the following statements about Km is false? The km for a substrate will vary depending on the conditions of the reaction The km is equal to ½ vmax The kcat of a reaction will vary as it is equal to Vmax/km Km reflects the stability of the enzyme-substrate complex Both B and C are false Both A and C are false Not sure if 5 or 6 is correctAn enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken). A mutation in the active site of an enzyme resulting in a large increase in…Which of the following statements is true about effect of substrate concentration on enzyme activity ? The rate of reaction increases as the substrate concentration increases up to certain limit at which the reaction rate is maximal (Vmax.) At Vmax, the enzyme is completely saturated with the substrate, At Vmax, any increase in substrate concentration don't affect the reaction rate. All of them
- What statement about states of the allosteric enzyme is TRUE? The value of KM for the T state is lower than for the R state. O The value of Vmax for the T state is lower than for the R state. O The value of KM for the T state and the R state is the same. The value of Vmax for the T state is higher than for the R state. O The value of KM for the T state is higher than for the R state.Which of the following statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.What does the Km of an enzyme measure? The affinity (strength of binding) of an enzyme for its substrate. The substrate concentration when AG is 0. The point at which activation energy is overcome. The amount of substrate needed to achieve Vmax- When half of the available enzyme is bound by substrate.
- The Michaelis constant: depends on the concentration of the enzyme. displays the maximal rate of the reaction, when it is much less than the substrate concentration. displays the maximal rate of the reaction, when it is equal to the substrate concentration. displays zero-order kinetics, when the it is equal to the substrate concentration. describes the properties of the enzyme.Which of the following is NOT true about enzymes? Enzyme inhibitors interact reversibly or irreversibly with an enzyme to alter its Km and /or Vmax values. Enzymes typically act under milder conditions of temperature and pH than non-enzyme chemical catalysts. Zymogens are the inactive precursors of enzyme. Nucleophilic groups can catalyze reactions through the transient formation of covalent bonds with the substrate. Transition state stabilization can significantly increase the activation energy for a reaction.Many pharmaceuticals exert their action by inhibiting the activity of enzymes. Choose the false statement regarding enzyme inhibition. A- Enzyme can be inhibited by a ligand that binds to an active site B- Enzyme can be inhibited by a ligand that binds to a site other than that of substrate C- Enzyme can be inhibited by a ligand that forms a covalent bond with enzyme. D- It is true of all enzyme inhibitors, that the degree of inhibition is reduced when the concentration of inhibitor is lowered by metabolism or E- Enzyme may be inhibited by a ligand that does not bind in the substrate site